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Protein

Cytochrome c oxidase subunit 2

Gene

COX2

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Status
Reviewed-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. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Cu cationBy similarityNote: Binds a copper A center.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi175Copper ABy similarity1
Metal bindingi210Copper ABy similarity1
Metal bindingi214Copper ABy similarity1
Metal bindingi218Copper ABy similarity1

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Respiratory chain, Transport
LigandCopper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 2 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c oxidase polypeptide II
Gene namesi
Name:COX2
Encoded oniMitochondrion
OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Taxonomic identifieri284592 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
Proteomesi
  • UP000000599 Componenti: Mitochondrion

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei31 – 51HelicalSequence analysisAdd BLAST21
Transmembranei72 – 92HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003550321 – 246Cytochrome c oxidase subunit 2Add BLAST246

Structurei

3D structure databases

ProteinModelPortaliA9RAG1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiA9RAG1
KOiK02261
OrthoDBiEOG092C40RV

Family and domain databases

CDDicd13912 CcO_II_C, 1 hit
Gene3Di1.10.287.90, 1 hit
2.60.40.420, 1 hit
InterProiView protein in InterPro
IPR002429 CcO_II-like_C
IPR034210 CcO_II_C
IPR001505 Copper_CuA
IPR008972 Cupredoxin
IPR014222 Cyt_c_oxidase_su2
IPR011759 Cyt_c_oxidase_su2_TM_dom
IPR036257 Cyt_c_oxidase_su2_TM_sf
PfamiView protein in Pfam
PF00116 COX2, 1 hit
PF02790 COX2_TM, 1 hit
SUPFAMiSSF49503 SSF49503, 1 hit
SSF81464 SSF81464, 1 hit
TIGRFAMsiTIGR02866 CoxB, 1 hit
PROSITEiView protein in PROSITE
PS00078 COX2, 1 hit
PS50857 COX2_CUA, 1 hit
PS50999 COX2_TM, 1 hit

Sequencei

Sequence statusi: Complete.

A9RAG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIWTDVPTPW GMRFQDAATP NAEGMHELYD HMMYYLALML GLVSYMLYVM
60 70 80 90 100
MKDYKNNTFA YKYIKHGQTL EIMWTMFPAV MLLLMAFPSF MLLYLCDEVL
110 120 130 140 150
TPAMTVKVVG LQWYWKYEYS DFVSETGETV EYESYVMPED MLEEGQLRLL
160 170 180 190 200
DTDTSMVVPV DTHVRFMVTA NDVLHCFTMP SLGIKVDACP GRLNQVSALM
210 220 230 240
QRTGVYYGQC SELCGVNHGL MPIKTECVPI GDFVEWLGEQ ENVYVA
Length:246
Mass (Da):28,359
Last modified:February 5, 2008 - v1
Checksum:i8F8982C0B23935B4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti223I → T in ABU80664 (PubMed:18248416).Curated1
Sequence conflicti223I → T in ABU80663 (PubMed:18248416).Curated1
Sequence conflicti223I → T in CAQ51421 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51422 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51423 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51424 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51428 (Ref. 3) Curated1
Sequence conflicti223I → T in CAQ51429 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti39M → V in strain: CBS 789 and CLIB 381. 2 Publications1
Natural varianti46M → L in strain: CLIB 660. 1 Publication1
Natural varianti51M → I in strain: CBS 789 and CLIB 381. 2 Publications1
Natural varianti106V → I in strain: CBS 789 and CLIB 381. 2 Publications1
Natural varianti179M → I in strain: CBS 789 and CLIB 381. 2 Publications1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ508940 Genomic DNA Translation: ABF58062.1
EF599377 Genomic DNA Translation: ABU80663.1
EF599378 Genomic DNA Translation: ABU80664.1
AM991984 Genomic DNA Translation: CAQ51421.1
AM991986 Genomic DNA Translation: CAQ51423.1
AM991987 Genomic DNA Translation: CAQ51424.1
AM991985 Genomic DNA Translation: CAQ51422.1
AM991991 Genomic DNA Translation: CAQ51428.1
AM991992 Genomic DNA Translation: CAQ51429.1
D55727 Genomic DNA Translation: BAA09541.1
RefSeqiYP_001621413.1, NC_010166.1

Genome annotation databases

GeneIDi5845854
KEGGidha:cox2

Similar proteinsi

Entry informationi

Entry nameiCOX2_DEBHA
AccessioniPrimary (citable) accession number: A9RAG1
Secondary accession number(s): B0LCE8
, B0LCE9, B4F4K1, B4F4K2, B4F4K4, B4F4K8, Q34322
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 5, 2008
Last modified: May 23, 2018
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health