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P29652 (COX1_POMNI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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
OrganismPomoxis nigromaculatus (Black crappie) (Cantharus nigromaculatus)
Taxonomic identifier8182 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPercomorphariaCentrarchiformesCentrarchidaePomoxis

Protein attributes

Sequence length161 AA.
Sequence statusFragment.
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

Chain‹1 – ›161›161Cytochrome c oxidase subunit 1
PRO_0000183401

Regions

Transmembrane4 – 2421Helical; Potential
Transmembrane38 – 5821Helical; Potential
Transmembrane80 – 10021Helical; Potential
Transmembrane108 – 12821Helical; Potential
Transmembrane141 – 16121Helical; Potential

Sites

Metal binding101Copper B Probable
Metal binding141Copper B Probable
Metal binding601Copper B Probable
Metal binding611Copper B Probable
Metal binding1461Iron (heme A3 axial ligand) Probable
Metal binding1481Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link10 ↔ 141'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1611

Sequences

Sequence LengthMass (Da)Tools
P29652 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: ADB0E64C3EF92EF2

FASTA16117,991
        10         20         30         40         50         60 
YQHLFWFFGH PEVYILILPG FGMISHIVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH 

        70         80         90        100        110        120 
HMFTVGMDVD TRAYFTSATM IIAIPTGVKV FSWLATLHGA SIKWETPLLW ALGFIFLFTV 

       130        140        150        160 
GGLTGIVLAN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIV A 

« Hide

References

[1]"Phylogenetic relationships of neopterygian fishes, inferred from mitochondrial DNA sequences."
Normark B.B., McCune A.R., Harrison R.G.
Mol. Biol. Evol. 8:819-834(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64914 Genomic DNA. Translation: AAB01478.1.

3D structure databases

ProteinModelPortalP29652.
SMRP29652. Positions 1-161.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_POMNI
AccessionPrimary (citable) accession number: P29652
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 11, 2014
This is version 85 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