Probable cytochrome c oxidase subunit 1 - Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)

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P63853 (COX1_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. 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:
Probable cytochrome c oxidase subunit 1
EC=1.9.3.1

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

Gene names

Name:	ctaD
Ordered Locus Names:	Mb3069c

Organism

Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]

Taxonomic identifier

233413 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›

Protein attributes

Sequence length	573 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	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
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 – 573

573

Probable cytochrome c oxidase subunit 1

PRO_0000183444

Regions

Transmembrane

40 – 60

Helical; Potential

Transmembrane

89 – 109

Helical; Potential

Transmembrane

121 – 141

Helical; Potential

Transmembrane

170 – 190

Helical; Potential

Transmembrane

213 – 233

Helical; Potential

Transmembrane

258 – 278

Helical; Potential

Transmembrane

290 – 310

Helical; Potential

Transmembrane

315 – 335

Helical; Potential

Transmembrane

359 – 379

Helical; Potential

Transmembrane

398 – 418

Helical; Potential

Transmembrane

433 – 453

Helical; Potential

Transmembrane

476 – 496

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

264

Copper B Probable

Metal binding

268

Copper B Probable

Metal binding

313

Copper B Probable

Metal binding

314

Copper B Probable

Metal binding

397

Iron (heme A3 axial ligand) Probable

Metal binding

399

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

264 ↔ 268

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

Sequences

Sequence

Length

Mass (Da)

Tools

P63853 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 9B0F91666F482BEE
Show »

FASTA

573

63,673

        10         20         30         40         50         60 
MTAEAPPLGE LEAIRPYPAR TGPKGSLVYK LITTTDHKMI GIMYCVACIS FFFIGGLLAL 

        70         80         90        100        110        120 
LMRTELAAPG LQFLSNEQFN QLFTMHGTIM LLFYATPIVF GFANLVLPLQ IGAPDVAFPR 

       130        140        150        160        170        180 
LNAFSFWLFV FGATIGAAGF ITPGGAADFG WTAYTPLTDA IHSPGAGGDL WIMGLIVAGL 

       190        200        210        220        230        240 
GTILGAVNMI TTVVCMRAPG MTMFRMPIFT WNIMVTSILI LIAFPLLTAA LFGLAADRHL 

       250        260        270        280        290        300 
GAHIYDAANG GVLLWQHLFW FFGHPEVYII ALPFFGIVSE IFPVFSRKPI FGYTTLVYAT 

       310        320        330        340        350        360 
LSIAALSVAV WAHHMFATGA VLLPFFSFMT YLIAVPTGIK FFNWIGTMWK GQLTFETPML 

       370        380        390        400        410        420 
FSVGFMVTFL LGGLTGVLLA SPPLDFHVTD SYFVVAHFHY VLFGTIVFAT FAGIYFWFPK 

       430        440        450        460        470        480 
MTGRLLDERL GKLHFWLTFI GFHTTFLVQH WLGDEGMPRR YADYLPTDGF QGLNVVSTIG 

       490        500        510        520        530        540 
AFILGASMFP FVWNVFKSWR YGEVVTVDDP WGYGNSLEWA TSCPPPRHNF TELPRIRSER 

       550        560        570 
PAFELHYPHM VERLRAEAHV GRHHDEPAMV TSS

« Hide

References

[1]

"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.

Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248344 Genomic DNA. Translation: CAD96756.1.
RefSeq	NP_856714.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P63853.
SMR	P63853. Positions 26-544.
ModBase	Search...
Protein-protein interaction databases
STRING	233413.Mb3069c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD96756; CAD96756; Mb3069c.
GeneID	1093667.
KEGG	mbo:Mb3069c.
PATRIC	18008482. VBIMycBov88188_3371.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0843.
HOGENOM	HOG000085275.
KO	K02274.
OMA	FGASLEW.
ProtClustDB	CLSK872133.
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_MYCBO

Accession

Primary (citable) accession number: P63853
Secondary accession number(s): O53290

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 66 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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents