Cytochrome c oxidase polypeptide 1 - Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)

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P33518 (COX1_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. History...

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

Documents (2) |

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 polypeptide 1
EC=1.9.3.1

Alternative name(s):
Cytochrome aa3 subunit 1
Cytochrome c oxidase polypeptide I

Gene names

Name:	coxA2
Ordered Locus Names:	VNG_0657G

Organism

Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP]

Taxonomic identifier

64091 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium ›

Protein attributes

Sequence length	593 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.
Subcellular location	Cell 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	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro 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 iron ion 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 – 593

593

Cytochrome c oxidase polypeptide 1

PRO_0000183465

Regions

Transmembrane

5 – 25

Helical; Potential

Transmembrane

71 – 91

Helical; Potential

Transmembrane

122 – 142

Helical; Potential

Transmembrane

154 – 174

Helical; Potential

Transmembrane

204 – 224

Helical; Potential

Transmembrane

246 – 266

Helical; Potential

Transmembrane

288 – 308

Helical; Potential

Transmembrane

320 – 340

Helical; Potential

Transmembrane

358 – 378

Helical; Potential

Transmembrane

401 – 421

Helical; Potential

Transmembrane

425 – 445

Helical; Potential

Transmembrane

467 – 487

Helical; Potential

Transmembrane

506 – 526

Helical; Potential

Sites

Metal binding

117

Iron (heme A axial ligand) Probable

Metal binding

294

Copper B Probable

Metal binding

298

Copper B Probable

Metal binding

343

Copper B Probable

Metal binding

344

Copper B Probable

Metal binding

429

Iron (heme A3 axial ligand) Probable

Metal binding

431

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

294 ↔ 298

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

Sequences

Sequence

Length

Mass (Da)

Tools

P33518 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: DCEC7CF007ACD326
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FASTA

593

65,294

        10         20         30         40         50         60 
MATAASSITL TVLMGVLLVG VVAVLARLED WRSYTPLSDV GGGLGERTGY THEEKPGGII 

        70         80         90        100        110        120 
RWFTTVDHKD IGILYGVYGT IAFAWGGVSV LLMRTELATS SETLISPSLY NGLLTSHGIT 

       130        140        150        160        170        180 
MLFLFGTPMI AAFGNYFIPL LIDADDMAFP RINAIAFWLL PPGAILIWSG FLIPGIATAQ 

       190        200        210        220        230        240 
TSWTMYTPLS LQMSSPAVDM MMLGLHLTGV SATMGAINFI ATIFTERGED VGWPDLDIFS 

       250        260        270        280        290        300 
WTMLTQSGLI LFAFPLFGSA LIMLLLDRNF GTTFFTVAGG DPIFWQHLFW FFGHPEVYVL 

       310        320        330        340        350        360 
VLPPMGIVSL ILPKFSGRKL FGFKFVVYST LAIGVLSFGV WAHHMFTTGI DPRIRSSFMA 

       370        380        390        400        410        420 
VSLAISIPSA VKVFNWITTM WNGKLRLTAP MLFCIGFVQN FIIGGVTGVF LAVIPIDLIL 

       430        440        450        460        470        480 
HDTYYVVGHF HFIVYGAIGF ALFAASYYWF PMVTGRMYQK RLAHAHFWTA LVGSNATFLA 

       490        500        510        520        530        540 
MLWLGYGGMP RRYATYIPQF ATAHRLATVG AFLIGVSTLI WLFNMATSWR EGPRVDSTDP 

       550        560        570        580        590 
WDLEETDQFT NDWAWFRAKE ETTVLPDGGD EAQSEADAVT DGGQPAADSD TES

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the cytochrome aa3 gene from the archaeon (Archaebacterium) Halobacterium halobium." Denda K., Fujiwara T., Seki M., Yoshida M., Fukumori Y., Yamanaka T. Biochem. Biophys. Res. Commun. 181:316-322(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Genome sequence of Halobacterium species NRC-1." Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. DasSarma S. Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700922 / JCM 11081 / NRC-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D10611 Genomic DNA. Translation: BAA01466.1. AE004437 Genomic DNA. Translation: AAG19154.1.
PIR	F84223. JT0974.
RefSeq	NP_279674.1. NC_002607.1.
3D structure databases
ProteinModelPortal	P33518.
ModBase	Search...
Protein-protein interaction databases
STRING	64091.VNG0657G.
Protein family/group databases
TCDB	3.D.4.3.1. proton-translocating cytochrome oxidase (COX) superfamily.
Proteomic databases
PaxDb	P33518.
PRIDE	P33518.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG19154; AAG19154; VNG_0657G.
GeneID	1447460.
KEGG	hal:VNG0657G.
Phylogenomic databases
eggNOG	COG0843.
KO	K02274.
OMA	HARKPLF.
ProtClustDB	CLSK511177.
Enzyme and pathway databases
UniPathway	UPA00705.
Family and domain databases
Gene3D	1.20.210.10. 1 hit.
InterPro	IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. IPR014241. Cyt_c_oxidase_su1_bac. [Graphical view]
PANTHER	PTHR10422. PTHR10422. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
SUPFAM	SSF81442. COX1. 1 hit.
TIGRFAMs	TIGR02891. CtaD_CoxA. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COX1_HALSA

Accession

Primary (citable) accession number: P33518
Secondary accession number(s): Q9HRK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

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

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

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents