[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=LO; DOI=10.1093/nar/18.20.6143; PubMed=2172930 [NCBI, ExPASy, EBI, Israel, Japan] Gabel C., Maier R.J.; "Nucleotide sequence of the coxA gene encoding subunit I of cytochrome aa3 of Bradyrhizobium japonicum."; Nucleic Acids Res. 18:6143-6143(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=USDA 110spc4; PubMed=1965217 [NCBI, ExPASy, EBI, Israel, Japan] Bott M., Bolliger M., Hennecke H.; "Genetic analysis of the cytochrome c-aa3 branch of the Bradyrhizobium japonicum respiratory chain."; Mol. Microbiol. 4:2147-2157(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=USDA 110spc4; Rossmann R., Loferer H., Rossi P., Hennecke H.; "Factors involved in biogenesis of active cytochrome aa3 encoded by the coxBAEFGC gene cluster from Bradyrhizobium japonicum."; Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=USDA 110spc4; Mueller P.; "Extended sequencing of a DNA fragment of B.japonicum adjacent to the cox operon."; Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=USDA 110; DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan] Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.; "Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."; DNA Res. 9:189-197(2002).

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.
DEVELOPMENTAL STAGE: Free in soil (not as bacteroid).
SIMILARITY: Belongs to the heme-copper respiratory oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X54318; CAA38216.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X54800; CAA38570.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ242592; CAB56819.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33883; AAF78815.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000040; BAC46436.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S13076; ODZJ1.

RefSeq

NP_767811.1; -.

3D structure databases

HSSP

P00396; 2OCC. [HSSP ENTRY / PDB]

ModBase

P31833.

Enzyme and pathway databases

BioCyc

BJAP224911:BLR1171-MON; -.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005746;	Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004129;	Molecular function: cytochrome-c oxidase activity (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0009060;	Biological process: aerobic respiration (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000883; COX1.
IPR014241; COX1_bac-type.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.210.10; COX1; 1.

PANTHER

PTHR10422; COX1; 1.

Pfam

PF00115; COX1; 1.
Pfam graphical view of domain structure.

PRINTS

PR01165; CYCOXIDASEI.

TIGRFAMs

TIGR02891; CtaD_CoxA; 1.

PROSITE

PS50855; COX1; 1.
PS00077; COX1_CUB; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P31833.

Genome annotation databases

GeneID

1049669; -.

GenomeReviews

BA000040_GR; blr1171.

KEGG

bja:blr1171; -.

NMPDR

fig|224911.1.peg.1171; -.

Phylogenomic databases

HOGENOM

P31833; -.

Genome annotation databases

CMR

P31833; blr1171.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Complete proteome; Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; Oxidoreductase; Respiratory chain; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 541`	`541`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183437`
`TRANSMEM`	`40 60`	`21`	`Potential.`
`TRANSMEM`	`87 107`	`21`	`Potential.`
`TRANSMEM`	`124 144`	`21`	`Potential.`
`TRANSMEM`	`173 193`	`21`	`Potential.`
`TRANSMEM`	`211 231`	`21`	`Potential.`
`TRANSMEM`	`262 282`	`21`	`Potential.`
`TRANSMEM`	`294 314`	`21`	`Potential.`
`TRANSMEM`	`332 352`	`21`	`Potential.`
`TRANSMEM`	`365 385`	`21`	`Potential.`
`TRANSMEM`	`404 424`	`21`	`Potential.`
`TRANSMEM`	`441 461`	`21`	`Potential.`
`TRANSMEM`	`483 503`	`21`	`Potential.`
`METAL`	`85 85`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`268 268`		`Copper B (Probable).`
`METAL`	`272 272`		`Copper B (Probable).`
`METAL`	`317 317`		`Copper B (Probable).`
`METAL`	`318 318`		`Copper B (Probable).`
`METAL`	`403 403`		`Iron (heme A3 axial ligand) (Probable).`
`METAL`	`405 405`		`Iron (heme A axial ligand) (Probable).`
`CROSSLNK`	`268 272`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`

Sequence information

Length: 541 AA [This is the length of the unprocessed precursor]

Molecular weight: 59265 Da [This is the MW of the unprocessed precursor]

CRC64: 08F9A69D0C90DB85 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATSAAAHGD HAQDHGHDEH AHPTGWRRYV YSTNHKDIGT MYLIFAVIAG VIGAAMSIAI 

        70         80         90        100        110        120 
RAELMYPGVQ IFHETHTYNV FVTSHGLIMI FFMVMPAMIG GFGNWFVPLM IGAPDMAFPR 

       130        140        150        160        170        180 
MNNISFWLLP ASFGLLLMST FVEGEPGANG VGAGWTMYVP LSSSGHPGPA VDFAILSLHL 

       190        200        210        220        230        240 
AGASSILGAI NFITTIFNMR APGMTLHKMP LFVWSILVTV FLLLLSLPVL AGAITMLLTD 

       250        260        270        280        290        300 
RNFGTTFFAP DGGGDPVLFQ HLFWFFGHPE VYILILPGFG MISQIVSTFS RKPVFGYLGM 

       310        320        330        340        350        360 
AYAMVAIGGI GFVVWAHHMY TVGMSSATQA YFVAATMVIA VPTGVKIFSW IATMWGGSIE 

       370        380        390        400        410        420 
FRAPMIWAVG FIFLFTVGGV TGVVLANAGV DRVLQETYYV VAHFHYVLSL GAVFAIFAGW 

       430        440        450        460        470        480 
YYWFPKMTGY MYNETLAKAH FWVTFIGVNL VFFPQHFLGL SGMPRRYVDY PDAFAGWNLV 

       490        500        510        520        530        540 
SSVGSYISGF GVLIFLYCVI DAFAKKVPAG DNPWGAGATT LEWTLPSPPP FHQFEVLPRV 


Q

P31833 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools