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P00398 (COX1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 1

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:mt-co1
Synonyms:coi, coxi, mtco1
Encoded onMitochondrion
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 519519Cytochrome c oxidase subunit 1
PRO_0000183430

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane56 – 7621Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane145 – 16521Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane234 – 25421Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane305 – 32521Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane412 – 43221Helical; Potential
Transmembrane456 – 47621Helical; Potential

Sites

Metal binding611Iron (heme A axial ligand) Probable
Metal binding2401Copper B Probable
Metal binding2441Copper B Probable
Metal binding2901Copper B Probable
Metal binding2911Copper B Probable
Metal binding3761Iron (heme A3 axial ligand) Probable
Metal binding3781Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P00398 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 23EDCD57B22F9A68

FASTA51957,440
        10         20         30         40         50         60 
MAITRWLFST NHKDIGTLYL VFGAWAGLVG TALSLLIRAE LSQPGTLLGD DQIYNVIVTA 

        70         80         90        100        110        120 
HAFIMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGISSILG AINFITTTIN MKPPAMSQYQ 

       190        200        210        220        230        240 
TPLFVWSVLI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPVL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GLLGFIVWAH HMFTVDLNVD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FSWLATMHGG TIKWDAPMLW ALGFIFLFTV GGLTGIVLAN 

       370        380        390        400        410        420 
SSLDIMLHDT YYVVAHFHYV LSMGAVFAIM GGFIHWFPLF TGYTLHETWA KIHFGVMFAG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLSAMPRRY SDYPDAYTLW NTVSSIGSLI SLVAVIMMMF IIWEAFAAKR 

       490        500        510 
EVTTYELTST MLEWLQGCPT PYHTLKTSLV QINHQMIKS 

« Hide

References

[1]"The complete nucleotide sequence of the Xenopus laevis mitochondrial genome."
Roe B.A., Ma D.-P., Wilson R.K., Wong J.F.-H.
J. Biol. Chem. 260:9759-9774(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10217 Genomic DNA. Translation: AAA66460.1.
PIRODXL1. A00466.
RefSeqNP_008136.1. NC_001573.1.

3D structure databases

ProteinModelPortalP00398.
SMRP00398. Positions 3-506.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2642088.
KEGGxla:2642088.

Organism-specific databases

CTD4512.
XenbaseXB-GENE-6251957. cox1.

Phylogenomic databases

HOVERGENHBG003841.
KOK02256.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_XENLA
AccessionPrimary (citable) accession number: P00398
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways