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Record Information
Version1.0
Creation Date2016-09-30 22:34:59 UTC
Update Date2020-05-19 22:01:32 UTC
BMDB IDBMDB0000692
Secondary Accession Numbers
  • BMDB00692
Metabolite Identification
Common NameIron
DescriptionIron, also known as fe (ii) ion or fe(ii), belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom. Iron exists as a solid, possibly soluble (in water), and possibly neutral molecule. Iron exists in all living species, ranging from bacteria to humans. Iron is a potentially toxic compound.
Structure
Thumb
Synonyms
ValueSource
FE (II) ionChEBI
Fe(II)ChEBI
Fe2+ChEBI
Fe(2+)ChEBI
Ferrous ionChEBI
Iron ion(2+)ChEBI
Iron(2+)Kegg
Armco ironHMDB
Carbonyl ironHMDB
FEHMDB
Ferrovac eHMDB
HematiteHMDB
InfedHMDB
LimoniteHMDB
LOHAHMDB
MagnetiteHMDB
Malleable ironHMDB
MetopironeHMDB
MetyraponeHMDB
PZH2mHMDB
PZHOHMDB
RemkoHMDB
Suy-b 2HMDB
TaconiteHMDB
VenoferHMDB
Wrought ironHMDB
Iron hydroxide (fe(OH)3)MeSH, HMDB
Iron oxyhydroxideMeSH, HMDB
Ferric hydroxideMeSH, HMDB
Iron hydroxide (III)MeSH, HMDB
Chemical FormulaFe
Average Molecular Weight55.845
Monoisotopic Molecular Weight55.934942133
IUPAC Namelambda2-iron(2+) ion
Traditional Namelambda2-iron(2+) ion
CAS Registry Number15438-31-0
SMILES
[Fe++]
InChI Identifier
InChI=1S/Fe/q+2
InChI KeyCWYNVVGOOAEACU-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.
KingdomInorganic compounds
Super ClassHomogeneous metal compounds
ClassHomogeneous transition metal compounds
Sub ClassNot Available
Direct ParentHomogeneous transition metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous transition metal
Molecular FrameworkNot Available
External Descriptors
Ontology
StatusDetected and Quantified
Origin
  • Exogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locationsNot Available
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP-0.77ChemAxon
pKa (Strongest Acidic)4.58ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity0 m³·mol⁻¹ChemAxon
Polarizability1.78 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleNoChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0a4i-9000000000-af3e7aec4f5bd9668683View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0a4i-9000000000-af3e7aec4f5bd9668683View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4i-9000000000-af3e7aec4f5bd9668683View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0udi-9000000000-3335fec4c3184739b75eView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0udi-9000000000-3335fec4c3184739b75eView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0udi-9000000000-3335fec4c3184739b75eView in MoNA
Biological Properties
Cellular LocationsNot Available
Biospecimen Locations
  • Blood
  • Brain
  • Liver
  • Longissimus Thoracis Muscle
  • Milk
  • Ruminal Fluid
  • Semimembranosus Muscle
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified52+/-13 uMNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
BrainExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
LiverExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
Longissimus Thoracis MuscleDetected and Quantified10+/-4 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
MilkDetected and Quantified5.372 - 12.535 uMNot SpecifiedNot SpecifiedNormal
    • Š. ZAMBERLIN et a...
details
MilkDetected and Quantified1.0314 - 13.597 uMNot SpecifiedNot SpecifiedNormal
    • Sola-Larrañaga C....
details
MilkDetected and Quantified14.325 uMNot SpecifiedNot SpecifiedNormal
    • Park, Y. W; Juáre...
details
MilkDetected and Quantified4 +/- 0.2 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4 +/- 0.3 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4 +/- 0.3 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4 +/- 0.5 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified39.395 +/- 1.791 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified23.279 +/- 1.791 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified41.185 +/- 1.791 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified33.127 +/- 1.433 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified44.767 +/- 89.534 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified14.683 +/- 1.433 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified8.953 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified8.953 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified7.163 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified7.163 - 8.953 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified8.953 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified8.953 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified10.744 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified8.953 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified10.744 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified8.953 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.551 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.551 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified8.953 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified10.744 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified8.953 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified10.744 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified3.581 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified3.581 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5.372 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified10.744 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified7.163 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified7.163 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified14.325 - 389.113 uMNot SpecifiedNot SpecifiedNormal
    • Semaghiul Birghil...
details
Ruminal FluidDetected and Quantified26.4 +/- 5.0 uMNot SpecifiedNot Specified
Normal
    • Fozia Saleem, Sou...
details
Ruminal FluidDetected and Quantified40+/-8 uMNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
Semimembranosus MuscleDetected and Quantified8+/-3 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
Abnormal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected but not QuantifiedNot ApplicableNot SpecifiedNot Specified
Fatal bovine respiratory disease
details
HMDB IDHMDB0015531
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB030855
KNApSAcK IDNot Available
Chemspider ID25394
KEGG Compound IDC14818
BioCyc IDFerric-Hydroxamate-Complexes
BiGG ID33552
Wikipedia LinkIron
METLIN IDNot Available
PubChem Compound27284
PDB IDFE2
ChEBI ID29033
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Gaucheron F: Milk and dairy products: a unique micronutrient combination. J Am Coll Nutr. 2011 Oct;30(5 Suppl 1):400S-9S. [PubMed:22081685 ]
  2. Semaghiul Birghila, Simona Dobrinas, Gabriela Stanciu and Alina Soceanu (2008). Semaghiul Birghila, Simona Dobrinas, Gabriela Stanciu and Alina Soceanu. Determination of major and minor elements in milk through ICP-AES. Environmental Engineering and Management Journal. November/December 2008, Vol.7, No.6, 805-808. Environmental Engineering and Management Journal.
  3. Park, Y. W; Juárez, Manuela ; Ramos, M.; Haenlein, G. F. W. (2007). Park, Y. W; Juárez, Manuela ; Ramos, M.; Haenlein, G. F. W.. Physico-chemical characteristics of goat and sheep milk. Small Ruminant Res.(2007) 68:88-113 doi: 10.1016/j.smallrumres.2006.09.013. Small Ruminant Research.
  4. A. Foroutan et al. (2019). A. Foroutan et al. The Chemical Composition of Commercial Cow's Milk (in preparation). Journal of Agricultural and Food Chemistry.
  5. Patricia Cava-Montesinos, M. Luisa Cervera Agustín Pastor Miguel de la Guardia (2005). Patricia Cava-Montesinos, M. Luisa Cervera Agustín Pastor Miguel de la Guardia. 2005. Room temperature acid sonication ICP-MS multielemental analysis of milk.Analytica Chimica Acta Volume 531, Issue 1, Pages 111-123. Analytica Chimica Acta.
  6. Šimun Zamberlin, Neven Antunac, Jasmina Havranek, Dubravka Samaržija (2012). Š. ZAMBERLIN et al.: Mineral elements in milk and dairy products, Mljekarstvo 62 (2), 111-125. Mljekarstvo.
  7. Cristina Sola-Larrañaga, Iñigo Navarro-Blasco (2009). Sola-Larrañaga C., Navarro-Blasco I. 2009. Chemometric analysis of minerals and trace elements in raw cow milk from the community of Navarra, Spain. Volume 112, Issue 1, Pages 189-196. Food Chemistry.
  8. USDA Food Composition Databases [Link]
  9. Fooddata+, The Technical University of Denmark (DTU) [Link]

Only showing the first 50 proteins. There are 184 proteins in total.

Enzymes

General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
MT-CO1
Uniprot ID:
P00396
Molecular weight:
57032.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively. Catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo/19-aldehyde derivatives, followed by a third oxidative aromatization step that involves C1-beta hydrogen abstraction combined with cleavage of the C10-C19 bond to yield a phenolic A ring and formic acid. Alternatively, the third oxidative reaction yields a 19-norsteroid and formic acid. Converts dihydrotestosterone to delta1,10-dehydro 19-nordihydrotestosterone and may play a role in homeostasis of this potent androgen. Also displays 2-hydroxylase activity toward estrone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Gene Name:
CYP19A1
Uniprot ID:
P46194
Molecular weight:
58090.0
General function:
Involved in cytochrome-c oxidase activity
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX5A
Uniprot ID:
P00426
Molecular weight:
16735.0
General function:
Involved in dopamine beta-monooxygenase activity
Specific function:
Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm.
Gene Name:
FRRS1
Uniprot ID:
A2VE04
Molecular weight:
65660.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
A cytochrome P450 monooxygenase involved in the biosynthesis of adrenal corticoids. Catalyzes the hydroxylation of carbon hydrogen bond at 11-beta position of 11-deoxycortisol and 11-deoxycorticosterone/21-hydroxyprogesterone yielding cortisol or corticosterone, respectively. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Gene Name:
CYP11B1
Uniprot ID:
P15150
Molecular weight:
57847.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
A cytochrome P450 monooxygenase involved in sterol biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25-dihydrolanosterol likely through sequential oxidative conversion of 14-alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed by the formation of the delta 14,15 double bond in the sterol core and concomitant release of formic acid. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Gene Name:
CYP51A1
Uniprot ID:
Q4PJW3
Molecular weight:
56596.0
General function:
Inorganic ion transport and metabolism
Specific function:
Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.
Gene Name:
CAT
Uniprot ID:
P00432
Molecular weight:
59915.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Gene Name:
CYP3A28
Uniprot ID:
P79102
Molecular weight:
58152.0
General function:
Energy production and conversion
Specific function:
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Gene Name:
MT-CYB
Uniprot ID:
P00157
Molecular weight:
42591.0
General function:
Energy production and conversion
Specific function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHC
Uniprot ID:
P35720
Molecular weight:
18389.0
General function:
Inorganic ion transport and metabolism
Specific function:
Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.
Gene Name:
NOS3
Uniprot ID:
P29473
Molecular weight:
133287.0
General function:
Energy production and conversion
Specific function:
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c.
Gene Name:
CYC1
Uniprot ID:
P00125
Molecular weight:
35297.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2).
Gene Name:
PTGIS
Uniprot ID:
Q29626
Molecular weight:
56629.0
General function:
Involved in heme binding
Specific function:
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Gene Name:
SDHD
Uniprot ID:
Q95123
Molecular weight:
17124.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMV6
Molecular weight:
20164.0
General function:
Involved in iron ion binding
Specific function:
Ferric-chelate reductase that reduces Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm. Probably uses ascorbate as electron donor (By similarity).
Gene Name:
CYB561A3
Uniprot ID:
A5D9A7
Molecular weight:
29803.0
General function:
Signal transduction mechanisms
Specific function:
Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP.
Gene Name:
GUCY1B1
Uniprot ID:
P16068
Molecular weight:
70502.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMT7
Molecular weight:
20837.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMS5
Molecular weight:
21961.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMS1
Molecular weight:
22058.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COI
Uniprot ID:
C5IS82
Molecular weight:
25404.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YN12
Molecular weight:
19067.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol. Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione. Has 16-alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates androgens, relevant for estriol synthesis. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Gene Name:
CYP17A1
Uniprot ID:
P05185
Molecular weight:
57244.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Gene Name:
CYP2D14
Uniprot ID:
Q01361
Molecular weight:
56083.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
A cytochrome P450 monooxygenase involved in the metabolism of arachidonic acid and its conjugates. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Acts as an omega and omega-1 hydroxylase for arachidonic acid and possibly for other long chain fatty acids. May modulate the arachidonic acid signaling pathway and play a role in other fatty acid signaling processes. May downregulate the biological activities of N-arachidonoyl-serotonin, an endocannabinoid that has anti-nociceptive effects through inhibition of fatty acid amide hydrolase FAAH, TRPV1 receptor and T-type calcium channels. Catalyzes C-2 oxidation of the indole ring of N-arachidonoyl-serotonin forming a less active product 2-oxo-N-arachidonoyl-serotonin.
Gene Name:
CYP2U1
Uniprot ID:
Q0IIF9
Molecular weight:
61997.0
General function:
Involved in heme binding
Specific function:
Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity).
Gene Name:
PTGS2
Uniprot ID:
O62698
Molecular weight:
69163.0
General function:
Involved in heme binding
Specific function:
Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells (By similarity).
Gene Name:
PTGS1
Uniprot ID:
O62664
Molecular weight:
68805.0
General function:
Involved in heme binding
Specific function:
Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide.
Gene Name:
CYBA
Uniprot ID:
O46521
Molecular weight:
20496.0
General function:
Involved in calcium ion binding
Specific function:
Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN). May protect the udder from infection and promote growth in newborn calves. Inhibits growth of the following bacterial species: E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus, S.epidermidis, and S.dysenteriae.
Gene Name:
LPO
Uniprot ID:
P80025
Molecular weight:
80642.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COI
Uniprot ID:
C5IS85
Molecular weight:
25438.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YN01
Molecular weight:
19520.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones (PubMed:11412116). Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R-hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal (PubMed:11412116). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin) (PubMed:11412116).
Gene Name:
CYP11A1
Uniprot ID:
P00189
Molecular weight:
60333.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Not Available
Gene Name:
CYP20A1
Uniprot ID:
Q5E980
Molecular weight:
52674.0
General function:
Involved in aromatase activity
Specific function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Gene Name:
Not Available
Uniprot ID:
P22779
Molecular weight:
2060.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMR7
Molecular weight:
22171.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Specifically catalyzes the 21-hydroxylation of steroids. Required for the adrenal synthesis of mineralocorticoids and glucocorticoids.
Gene Name:
CYP21
Uniprot ID:
P00191
Molecular weight:
56077.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COXI
Uniprot ID:
A5YMW7
Molecular weight:
19834.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics.
Gene Name:
CYP2E1
Uniprot ID:
O18963
Molecular weight:
56827.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COI
Uniprot ID:
A1XP62
Molecular weight:
8746.0
General function:
Energy production and conversion
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX1
Uniprot ID:
B1NZU1
Molecular weight:
57018.0
General function:
Coenzyme transport and metabolism
Specific function:
NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS) (By similarity).
Gene Name:
CYB5R4
Uniprot ID:
Q32LH7
Molecular weight:
59274.0
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the ferrous insertion into protoporphyrin IX.
Gene Name:
FECH
Uniprot ID:
P22600
Molecular weight:
46935.0
Reactions
Protoporphyrin IX + Iron → Heme +2 Hydrogendetails
General function:
Involved in holocytochrome-c synthase activity
Specific function:
Links covalently the heme group to the apoprotein of cytochrome c.
Gene Name:
HCCS
Uniprot ID:
A5PJG7
Molecular weight:
31069.0
General function:
Inorganic ion transport and metabolism
Specific function:
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of proinflammatory mediators such as IL6 and IL8.
Gene Name:
NOS2
Uniprot ID:
Q27995
Molecular weight:
131208.0
General function:
Involved in heme oxygenase (decyclizing) activity
Specific function:
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Gene Name:
HMOX1
Uniprot ID:
Q5E9F2
Molecular weight:
32940.0
General function:
Energy production and conversion
Specific function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Gene Name:
NDUFS7
Uniprot ID:
P42026
Molecular weight:
23771.0
General function:
Energy production and conversion
Specific function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Gene Name:
NDUFS2
Uniprot ID:
P17694
Molecular weight:
52556.0
General function:
Involved in iron ion binding
Specific function:
Not Available
Gene Name:
Not Available
Uniprot ID:
A9ZTK8
Molecular weight:
14355.0
General function:
Signal transduction mechanisms
Specific function:
Not Available
Gene Name:
PPP3CC
Uniprot ID:
A5D7T5
Molecular weight:
58180.0
General function:
Involved in iron ion binding
Specific function:
Not Available
Gene Name:
PPP3CB
Uniprot ID:
A6H703
Molecular weight:
59097.0

Only showing the first 50 proteins. There are 184 proteins in total.