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A9RAH5 (COX1_DEBHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:COX1
Encoded onMitochondrion
OrganismDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) [Complete proteome]
Taxonomic identifier284592 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Debaryomyces ›

Protein attributes

Sequence length536 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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 536536Cytochrome c oxidase subunit 1
PRO_0000355031

Regions

Transmembrane19 – 3921Helical; Potential
Transmembrane69 – 8921Helical; Potential
Transmembrane103 – 12321Helical; Potential
Transmembrane152 – 17221Helical; Potential
Transmembrane188 – 20821Helical; Potential
Transmembrane240 – 26021Helical; Potential
Transmembrane273 – 29321Helical; Potential
Transmembrane315 – 33521Helical; Potential
Transmembrane341 – 36121Helical; Potential
Transmembrane388 – 40821Helical; Potential
Transmembrane418 – 43821Helical; Potential
Transmembrane461 – 48121Helical; Potential

Sites

Metal binding671Iron (heme A axial ligand) By similarity
Metal binding2461Copper B By similarity
Metal binding2501Copper B By similarity
Metal binding2951Copper B By similarity
Metal binding2961Copper B By similarity
Metal binding3811Iron (heme A3 axial ligand) By similarity
Metal binding3831Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link246 ↔ 2501'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
A9RAH5 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 28EB8CDB07797510

FASTA53659,959
        10         20         30         40         50         60 
MKQMSYVTRW LYSTSHKDIG MTYLGFGMLS AMMGTGMSVM MRMELSNGNS QFFHGNNQAF 

        70         80         90        100        110        120 
NVMMSGHALL MMFFFIMPVW MGAFGNFFLP MLMGAADMAF ARLNNISFWC LPPALVCMVC 

       130        140        150        160        170        180 
SVLMEQGAGT GFTTYPPLSS MSAHSGPSVD LAMFAMHLTS MSSLLGAMNF MVTVLNMRTM 

       190        200        210        220        230        240 
GLHMVNMPLF AWAMFLTAML LLLSLPVLTA AVTLLLMDRN FNTGFYEVGA GGDPVTYEHL 

       250        260        270        280        290        300 
FWFFGHPEVY ILMMPGFGVM SHMVSTYSKK PMFGEMGMLY AMGSIGFLGF LVWSHHMFVV 

       310        320        330        340        350        360 
GLDIDSRAYF TSATMVIAVP TGIKIFSWLA TIYGGELRLG VPMLFALGFL FLFTMGGLTG 

       370        380        390        400        410        420 
VMTSNASMDV AFHDTYYVVG HFHYVLSMGA LFSLMGAYYY WGPAMFGLKY NRMLGEMHFW 

       430        440        450        460        470        480 
LLFMSVNVMF LPMHFLGLNG MPRRMPQYPD AFMGWNYMSS MGSAMSVMSV LVGLKSVLVQ 

       490        500        510        520        530 
LENGENEELE MQVTPDFTES NLNREIRDSD LDLILTRPAE YHTYSELPVL TSNSHA

« Hide

References

[1]"Promiscuous DNA in the nuclear genomes of hemiascomycetous yeasts."
Sacerdot C., Casaregola S., Lafontaine I., Tekaia F., Dujon B., Ozier-Kalogeropoulos O.
FEMS Yeast Res. 8:846-857(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ508940 Genomic DNA. Translation: ABF58076.1.
RefSeqYP_001621427.1. NC_010166.1.

3D structure databases

ProteinModelPortalA9RAH5.
ModBaseSearch...

Protein-protein interaction databases

STRING4959.A9RAH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5845853.
KEGGdha:cox1.

Phylogenomic databases

KOK02256.
OrthoDBEOG4BK8C4.

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. COX1. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_DEBHA
AccessionPrimary (citable) accession number: A9RAH5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: February 5, 2008
Last modified: May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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