Cytochrome c oxidase subunit 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P00401 (COX1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 110. History...

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

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Synonyms:	OXI3
Ordered Locus Names:	Q0045

Encoded on

Mitochondrion

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	534 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.
Subunit structure	Cytochrome c oxidase is composed of 11 subunits: one copy each of COX1, COX2, COX3, COX4, COX5A or COX5B, COX6, COX7, COX9, COX12, COX13 and two copies of COX8.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein.
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 Transmembrane helix
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from mutant phenotype. Source: SGD mitochondrial electron transport, cytochrome c to oxygen Inferred from direct assay. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial respiratory chain complex IV Inferred from physical interaction. Source: SGD
Molecular function	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 – 534

534

Cytochrome c oxidase subunit 1

PRO_0000183432

Regions

Transmembrane

16 – 38

Helical; Potential

Transmembrane

58 – 80

Helical; Potential

Transmembrane

101 – 123

Helical; Potential

Transmembrane

148 – 170

Helical; Potential

Transmembrane

183 – 205

Helical; Potential

Transmembrane

237 – 259

Helical; Potential

Transmembrane

266 – 288

Helical; Potential

Transmembrane

303 – 325

Helical; Potential

Transmembrane

337 – 359

Helical; Potential

Transmembrane

374 – 396

Helical; Potential

Transmembrane

409 – 431

Helical; Potential

Transmembrane

451 – 473

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

241

Copper B Probable

Metal binding

245

Copper B Probable

Metal binding

290

Copper B Probable

Metal binding

291

Copper B Probable

Metal binding

376

Iron (heme A3 axial ligand) Probable

Metal binding

378

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

241 ↔ 245

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

Experimental info

Sequence conflict

Missing in CAA24070. Ref.1

Sequence conflict

F → CT in CAA24070. Ref.1

Sequence conflict

224

S → A in CAA24070. Ref.1

Sequence conflict

328

H → Y in CAA24070. Ref.1

Sequence conflict

378

H → Y in CAA24070. Ref.1

Sequence conflict

479 – 485

Missing in CAA24070. Ref.1

Sequence conflict

492

N → A in CAA24070. Ref.1

Sequence conflict

496 – 510

Missing in CAA24070. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P00401 [UniParc].

Last modified April 23, 2003. Version 2.
Checksum: 5D555084C127E8B1
Show »

FASTA

534

58,798

        10         20         30         40         50         60 
MVQRWLYSTN AKDIAVLYFM LAIFSGMAGT AMSLIIRLEL AAPGSQYLHG NSQLFNVLVV 

        70         80         90        100        110        120 
GHAVLMIFFL VMPALIGGFG NYLLPLMIGA TDTAFPRINN IAFWVLPMGL VCLVTSTLVE 

       130        140        150        160        170        180 
SGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GAINFIVTTL NMRTNGMTMH 

       190        200        210        220        230        240 
KLPLFVWSIF ITAFLLLLSL PVLSAGITML LLDRNFNTSF FEVSGGGDPI LYEHLFWFFG 

       250        260        270        280        290        300 
HPEVYILIIP GFGIISHVVS TYSKKPVFGE ISMVYAMASI GLLGFLVWSH HMYIVGLDAD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGIKI FSWLATIHGG SIRLATPMLY AIAFLFLFTM GGLTGVALAN 

       370        380        390        400        410        420 
ASLDVAFHDT YYVVGHFHYV LSMGAIFSLF AGYYYWSPQI LGLNYNEKLA QIQFWLIFIG 

       430        440        450        460        470        480 
ANVIFFPMHF LGINGMPRRI PDYPDAFAGW NYVASIGSFI ATLSLFLFIY ILYDQLVNGL 

       490        500        510        520        530 
NNKVNNKSVI YNKAPDFVES NTIFNLNTVK SSSIEFLLTS PPAVHSFNTP AVQS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Assembly of the mitochondrial membrane system. Structure and nucleotide sequence of the gene coding for subunit 1 of yeast cytochrome oxidase." Bonitz S.G., Coruzzi G., Thalenfeld B.E., Tzagoloff A., Macino G. J. Biol. Chem. 255:11927-11941(1980) [PubMed: 6254986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 24657 / D273-10B.
[2]	"The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae." Foury F., Roganti T., Lecrenier N., Purnelle B. FEBS Lett. 440:325-331(1998) [PubMed: 9872396] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Sequence of the yeast mitochondrial OX13/OL12 promoter region." Seraphin B., Simon M., Jacq C., Faye G. Nucleic Acids Res. 17:4886-4886(1989) [PubMed: 2664712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56. Strain: ATCC 24657 / D273-10B.
[4]	"Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method." Geier B.M., Schagger H., Ortwein C., Link T.A., Hagen W.R., Brandt U., Von Jagow G. Eur. J. Biochem. 227:296-302(1995) [PubMed: 7851399] [Abstract] Cited for: COMPOSITION OF THE CYTOCHROME C OXIDASE COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	V00694 Genomic DNA. Translation: CAA24070.1. AJ011856 Genomic DNA. Translation: CAA09824.1. X14910 Genomic DNA. Translation: CAA33036.1.
PIR	ODBY1. A00468. S78640.
RefSeq	NP_009305.1. NM_001184352.1.
3D structure databases
ProteinModelPortal	P00401.
SMR	P00401. Positions 2-534.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00401. 1 interaction.
MINT	MINT-4981480.
STRING	P00401.
Protein family/group databases
TCDB	3.D.4.8.1. proton-translocating cytochrome oxidase (COX) superfamily.
Proteomic databases
PeptideAtlas	P00401.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	Q0045; Q0045; Q0045.
GeneID	854598.
KEGG	sce:Q0045.
NMPDR	fig\|4932.3.peg.1859.
Organism-specific databases
CYGD	Q0045.
SGD	S000007260. COX1.
Phylogenomic databases
eggNOG	fuNOG07675.
HOGENOM	HBG603668.
OrthoDB	EOG4BK8C4.
Gene expression databases
ArrayExpress	P00401.
Genevestigator	P00401.
GermOnline	Q0045. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. [Graphical view]
Gene3D	G3DSA:1.20.210.10. COX1. 1 hit.
KO	K02256.
PANTHER	PTHR10422. COX1. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
SUPFAM	SSF81442. COX1. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977080.

Entry information

Entry name

COX1_YEAST

Accession

Primary (citable) accession number: P00401
Secondary accession number(s): Q9ZZX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 23, 2003
Last modified:	December 14, 2011
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents