Reviewed, UniProtKB/Swiss-Prot P0C8K9 (COX1_CANAL)

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
ORF Names:	CaalfMp08

Encoded on

Mitochondrion

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

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
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 531	531	Cytochrome c oxidase subunit 1		PRO_0000356866
Regions
	Transmembrane	18 – 38	21	Potential
	Transmembrane	59 – 79	21	Potential
	Transmembrane	103 – 123	21	Potential
	Transmembrane	149 – 169	21	Potential
	Transmembrane	185 – 205	21	Potential
	Transmembrane	237 – 257	21	Potential
	Transmembrane	269 – 289	21	Potential
	Transmembrane	312 – 332	21	Potential
	Transmembrane	340 – 360	21	Potential
	Transmembrane	385 – 405	21	Potential
	Transmembrane	414 – 434	21	Potential
	Transmembrane	458 – 478	21	Potential
Sites
	Metal binding	64	1	Iron (heme A axial ligand) By similarity
	Metal binding	243	1	Copper B By similarity
	Metal binding	247	1	Copper B By similarity
	Metal binding	292	1	Copper B By similarity
	Metal binding	293	1	Copper B By similarity
	Metal binding	378	1	Iron (heme A3 axial ligand) By similarity
	Metal binding	380	1	Iron (heme A axial ligand) By similarity
Amino acid modifications
	Cross-link	243 ↔ 247		1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C8K9-1 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: EDB63911A328C6AA	FASTA	531	58,744
	10 20 30 40 50 60 MSYVTRWLFS TSHKDIGILY LIYGMVSAMV ATGMSVIIRL ELSGPGPMFL HGNNQVFNVL 70 80 90 100 110 120 VTGHAIAMIF LFVMPILIGS FGNYFLPIMI GAVDMAFARL NNISFWCLPP ALVCVIASVL 130 140 150 160 170 180 IETGAGTGWT VYPPLSSISA HSGPSVDLAI FAIHLTSISS LLGAINFIVT TLNMRSIGIH 190 200 210 220 230 240 MIDMPLFVWA IFFTAILLLL SLPVLTAGVT LLLMDRNFNT GFYEVAAGGD PILYEHLFYF 250 260 270 280 290 300 FGHPEVYIII IPGFGIISHV ISTYTKKPIF GQIGMIYAIG SIGLLGFLVW SHHMYVVGLD 310 320 330 340 350 360 IDSRAYFTSA TMVIAIPTGI KIFSWLATLY GGELRLAVPM LFALGFLFLF TIGGLTGVML 370 380 390 400 410 420 SNASIDVAFH DTYYVVGHFH YVLSMGALFS LIAGYYYWGP AMFGLKYNKV LAEVHYWLLF 430 440 450 460 470 480 VSVNIIFLPM HFLGLNGMPR RIPQYPDAFV GWNVVSSWGS IMSVISVLIG LYSVLVQLTN 490 500 510 520 530 GENEREEIQV TPDYLESNNT RDVRDSDLEL ITSRPAQYHT FSELPILIQQ I

References

[1]

"Infrequent genetic exchange and recombination in the mitochondrial genome of Candida albicans." Anderson J.B., Wickens C., Khan M., Cowen L.E., Federspiel N.A., Jones T., Kohn L.M. J. Bacteriol. 183:865-872(2001) [PubMed: 11208783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF285261 Genomic DNA. No translation available.
3D structure databases
ModBase	Search...
Organism-specific databases
CGD	CAF0007377. COX1.
Phylogenomic databases
OrthoDB	EOG9KPVV3.
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...

Entry information

Entry name

COX1_CANAL

Accession

Primary (citable) accession number: P0C8K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	December 16, 2008
Last modified:	November 24, 2009
This is version 8 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)