Cytochrome c oxidase subunit 1 - Ashbya gossypii (Yeast)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P62514 (COX1_ASHGO)

Last modified January 19, 2010. Version 41. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Cytochrome c oxidase subunit 1
    EC=1.9.3.1
Alternative name(s):
    Cytochrome c oxidase polypeptide I

Gene names

Name:	COX1
Ordered Locus Names:	AMI002W
ORF Names:	AgCOX1

Encoded on

Mitochondrion

Organism

Ashbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

33169 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

Hide | Top

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-KW respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 535

535

Cytochrome c oxidase subunit 1

PRO_0000183289

Regions

Transmembrane

15 – 37

Potential

Transmembrane

58 – 80

Potential

Transmembrane

147 – 169

Potential

Transmembrane

190 – 212

Potential

Transmembrane

238 – 260

Potential

Transmembrane

267 – 289

Potential

Transmembrane

304 – 326

Potential

Transmembrane

339 – 361

Potential

Transmembrane

376 – 398

Potential

Transmembrane

415 – 437

Potential

Transmembrane

452 – 474

Potential

Sites

Metal binding

Iron (heme A axial ligand) By similarity

Metal binding

242

Copper B By similarity

Metal binding

246

Copper B By similarity

Metal binding

291

Copper B By similarity

Metal binding

292

Copper B By similarity

Metal binding

377

Iron (heme A3 axial ligand) By similarity

Metal binding

379

Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link

242 ↔ 246

1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P62514-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: BBEC610E44873A2C
Show »

FASTA

535

60,173

        10         20         30         40         50         60 
MYLQRWLFST NAKDIAILYF IFSTFCGLAG TAMSFIIRME LSAPGQQYLQ GQNQLFNVLV 

        70         80         90        100        110        120 
TGHTILMVFF LVMPMLIGGF GNYYLPLMIG ASDMSFARLN NISFWTLPPT LICLLTSTMV 

       130        140        150        160        170        180 
ESGTGTGWTV YPPLSSIQSH SGASVDLAIF SLHLTTISSL LGTINFIVTA LNMRTNGMTL 

       190        200        210        220        230        240 
HKMPLFTWSI LITAVMLLMS LPVLSAGVTM LLMDRNFNTS FFEVQGGGDP ILYQHLFWFF 

       250        260        270        280        290        300 
GHPEVYIMIV PTFGMMSHIV STYSKKPVFG EISMIYTMGS ISLLGFLVWS HHMYVVGLDT 

       310        320        330        340        350        360 
DTRAYFTSAT MIITIPTSIK VFSWLTTIYG GSLRLTTPML YTLSFLFLFT VGGLTGVVLA 

       370        380        390        400        410        420 
NTSLDVAFHD TYYVVTHFHY VLSLGAVFSM FAGYYYWSPT VLGLNYNEKL SQIQFWLIFL 

       430        440        450        460        470        480 
GTNIIFFPMH FLGINGMPRR IPDYPDTFTG WNLVSSFGSM MTIMSLMLFT YIIYDQLMNG 

       490        500        510        520        530 
LTNKVNNKSI NYMKTPDFIE SNNIFLMNTT KSSSIEFMLN SPPTIHSFNT PTIQS

« Hide

Hide | Top

References

[1]

"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed: 15001715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016821 Genomic DNA. Translation: AAS50169.1.
RefSeq	NP_987079.1.
3D structure databases
SMR	P62514. Positions 1-532.
ModBase	Search...
Protein-protein interaction databases
STRING	P62514.
Genome annotation databases
GeneID	2760766.
GenomeReviews	Gene locus AMI002W in contig AE016821_GR.
KEGG	ago:AGOS_AMI002W.
NMPDR	fig\|33169.1.peg.4720.
Organism-specific databases
AGD	AMI002W.
Phylogenomic databases
eggNOG	fuNOG07675.
HOGENOM	HBG603668.
OrthoDB	EOG9KPVV3.
Enzyme and pathway databases
BioCyc	AGOS-XXX-01:AGOS-XXX-01-004720-MONOMER.
BRENDA	1.9.3.1. 279361.
Family and domain databases
InterPro	IPR000883. Cyt_c_oxidase_su1. [Graphical view]
Gene3D	G3DSA:1.20.210.10. COX1. 1 hit.
PANTHER	PTHR10422. COX1. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Hide | Top

Entry information

Entry name

COX1_ASHGO

Accession

Primary (citable) accession number: P62514
Secondary accession number(s): Q75G35

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	January 19, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents