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Q96000 (COX1_PECMA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. 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:COI
Encoded onMitochondrion
OrganismPecten maximus (King scallop) (Pilgrim's clam)
Taxonomic identifier6579 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPectinoidaPectinoideaPectinidaePecten

Protein attributes

Sequence length477 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

Chain1 – ›477›477Cytochrome c oxidase subunit 1
PRO_0000183385

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane64 – 8421Helical; Potential
Transmembrane101 – 12121Helical; Potential
Transmembrane149 – 17123Helical; Potential
Transmembrane185 – 20521Helical; Potential
Transmembrane236 – 25621Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane309 – 32921Helical; Potential
Transmembrane340 – 36021Helical; Potential
Transmembrane382 – 40221Helical; Potential
Transmembrane416 – 43621Helical; Potential
Transmembrane455 – 47521Helical; Potential

Sites

Metal binding621Iron (heme A axial ligand) Probable
Metal binding2421Copper B Probable
Metal binding2461Copper B Probable
Metal binding2921Copper B Probable
Metal binding2931Copper B Probable
Metal binding3781Iron (heme A3 axial ligand) Probable
Metal binding3801Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link242 ↔ 2461'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Non-terminal residue4771

Sequences

Sequence LengthMass (Da)Tools
Q96000 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 4A6DA9D830CABAEE

FASTA47753,692
        10         20         30         40         50         60 
MVRWSRWFMA NSHKDVGTMY LMLGMWSGFG GLNLSWMMRL ELSRPGMWLP SSEVYNGIVT 

        70         80         90        100        110        120 
LHAIMMIFSF VMPVLIGGFG NWLLPMMLGS IDMSFPRLNT FSFWVLPPAL YLVIVSCFID 

       130        140        150        160        170        180 
YGSGTGWTMY PVPLSSTPYS GGISTDLMIL GLHLAGISSS AESINYLVTF LNVRSKSFKA 

       190        200        210        220        230        240 
EFSPLFVWAL AVTSFLLLVS LPVLAGGLTM LIMDRDFNCS FFDPSGGGDP VLFQHLFWFF 

       250        260        270        280        290        300 
GHPEVYVLIL PGFGLVSHVL VFYTKKLRVF GSVAMMYAMI SIGVLGFIVW GHHMYTVGLD 

       310        320        330        340        350        360 
VDTRFYFTAV TMLIAVPTGV KVFSWIATIY GSYLSFEAPT LWVLGFIMKF TMGGITGVIL 

       370        380        390        400        410        420 
SNACLDVALH DTYYVVAHFH YVLSMGAVFT IFAGYIHYFP FFTSKLFSPV LARGHFFLTF 

       430        440        450        460        470 
VGVNLTFFPQ HFLGLGGMPR RIPDYPIFYY YWNQWSTIGC AMVMVSVSLF IHMQWEA 

« Hide

References

[1]"Molecular cloning and complete nucleotide sequence of the repeated unit and flanking gene of the scallop Pecten maximus mitochondrial DNA: putative replication origin features."
Rigaa A., Monnerot M., Sellos D.
J. Mol. Evol. 41:189-195(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92688 Genomic DNA. Translation: CAA63370.1.

3D structure databases

ProteinModelPortalQ96000.
SMRQ96000. Positions 3-473.
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_PECMA
AccessionPrimary (citable) accession number: Q96000
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways