Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytochrome c oxidase subunit 1

Gene
N/A
Organism
Ridgeia piscesae (Tubeworm)
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

Pathwayi: oxidative phosphorylation

This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway oxidative phosphorylation and in Energy metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotation
Biological processElectron transport, Respiratory chainUniRule annotation, Transport
LigandCopperUniRule annotation, HemeUniRule annotation, Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00705

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 1UniRule annotation (EC:1.9.3.1UniRule annotation)
Encoded oniMitochondrionImported
OrganismiRidgeia piscesae (Tubeworm)Imported
Taxonomic identifieri27915 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaPalpataCanalipalpataSabellidaSiboglinidaeRidgeia

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membraneUniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ95941
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 214COX1InterPro annotationAdd BLAST214

Sequence similaritiesi

Belongs to the heme-copper respiratory oxidase family.UniRule annotation

Keywords - Domaini

TransmembraneUniRule annotation

Family and domain databases

Gene3Di1.20.210.10, 1 hit
InterProiView protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
PANTHERiPTHR10422 PTHR10422, 1 hit
PfamiView protein in Pfam
PF00115 COX1, 1 hit
PRINTSiPR01165 CYCOXIDASEI
SUPFAMiSSF81442 SSF81442, 1 hit
PROSITEiView protein in PROSITE
PS50855 COX1, 1 hit

Sequencei

Sequence statusi: Fragment.

Q95941-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LVGIWTGLVA TSMSLLIRAE LGQPGTLLGD DQIYNCLITA HGLLMMFFVV
60 70 80 90 100
LPILMGGFGN WLVPLMLGAP DMAFPRINNL GFWLIPPAVI LLVMSAFIEK
110 120 130 140 150
GAGTGWTVYP PLASNIAHAG PCIDLAIFAL HLSGVSSILA SINFITTVMN
160 170 180 190 200
MRYKGLRLER VPLFVWSVKL TAVLLLLSIP VLAGGLTMLL TDRNLNTSFF
210
DPAGGGDPVL YQPL
Length:214
Mass (Da):22,978
Last modified:June 1, 1998 - v2
Checksum:iD9910C52257B19AE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei1Imported1
Non-terminal residuei214Imported1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U74073 Genomic DNA Translation: AAC01527.1

Similar proteinsi

Entry informationi

Entry nameiQ95941_RIDPI
AccessioniPrimary (citable) accession number: Q95941
Entry historyiIntegrated into UniProtKB/TrEMBL: February 1, 1997
Last sequence update: June 1, 1998
Last modified: May 23, 2018
This is version 83 of the entry and version 2 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health