[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1007/s002030100262; PubMed=11382224 [NCBI, ExPASy, EBI, Israel, Japan] Niebisch A., Bott M.; "Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium glutamicum respiratory chain containing an unusual diheme cytochrome c1."; Arch. Microbiol. 175:282-294(2001).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, HEME CHARACTERIZATION, AND MASS SPECTROMETRY. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; PubMed=11577165 [NCBI, ExPASy, EBI, Israel, Japan] Sakamoto J., Shibata T., Mine T., Miyahara R., Torigoe T., Noguchi S., Matsushita K., Sone N.; "Cytochrome c oxidase contains an extra charged amino acid cluster in a new type of respiratory chain in the amino acid-producing Gram-positive bacterium Corynebacterium glutamicum."; Microbiology 147:2865-2871(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; Nakagawa S.; "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."; J. Biotechnol. 104:5-25(2003).
[5]	DETECTION IN A SUPERCOMPLEX WITH MENAQUINOL-CYTOCHROME C REDUCTASE (CYTOCHROME BC1). STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1074/jbc.M210499200; PubMed=12446663 [NCBI, ExPASy, EBI, Israel, Japan] Niebisch A., Bott M.; "Purification of a cytochrome bc1-aa3 supercomplex with quinol oxidase activity from Corynebacterium glutamicum. Identification of a fourth subunity of cytochrome aa3 oxidase and mutational analysis of diheme cytochrome c1."; J. Biol. Chem. 278:4339-4346(2003).

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.
COFACTOR: Binds 1 copper B per subunit (By similarity).
COFACTOR: Binds 2 heme groups per subunit (By similarity).
PATHWAY: Energy metabolism; oxidative phosphorylation .
SUBUNIT: Associates with subunits II, III and IV to form cytochrome c oxidase. The 4 subunit cytochrome c oxidase forms a supercomplex with the menaquinol-cytochrome c reductase complex (cytochrome bc1).
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
MASS SPECTROMETRY: Mass=64955.8; Mass_error=164.1; Method=MALDI; Range=1-584; Source=PubMed:11577165;.
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

AJ306417; CAC33824.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB052748; BAB64406.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAB99916.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927155; CAF21186.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_601724.2; -.
YP_226765.1; -.

3D structure databases

HSSP

P18401; 1FFT. [HSSP ENTRY / PDB]

ModBase

Q79VD7.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG2780-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

Q79VD7.

Genome annotation databases

GeneID

1020472; -.
3344025; -.

GenomeReviews

BX927147_GR; cg2780.
BA000036_GR; Cgl2523.

KEGG

cgb:cg2780; -.
cgl:NCgl2437; -.

Phylogenomic databases

HOGENOM

Q79VD7; -.

Genome annotation databases

CMR

Q79VD7; Cgl2523.

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`	`1 584`	`584`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183440`
`TRANSMEM`	`43 63`	`21`	`Potential.`
`TRANSMEM`	`90 110`	`21`	`Potential.`
`TRANSMEM`	`122 142`	`21`	`Potential.`
`TRANSMEM`	`171 191`	`21`	`Potential.`
`TRANSMEM`	`214 234`	`21`	`Potential.`
`TRANSMEM`	`259 279`	`21`	`Potential.`
`TRANSMEM`	`292 312`	`21`	`Potential.`
`TRANSMEM`	`316 336`	`21`	`Potential.`
`TRANSMEM`	`360 380`	`21`	`Potential.`
`TRANSMEM`	`399 419`	`21`	`Potential.`
`TRANSMEM`	`434 454`	`21`	`Potential.`
`TRANSMEM`	`477 497`	`21`	`Potential.`
`METAL`	`87 87`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`265 265`		`Copper B (Probable).`
`METAL`	`269 269`		`Copper B (Probable).`
`METAL`	`314 314`		`Copper B (Probable).`
`METAL`	`315 315`		`Copper B (Probable).`
`METAL`	`398 398`		`Iron (heme A3 axial ligand) (Probable).`
`METAL`	`400 400`		`Iron (heme A axial ligand) (Probable).`
`CROSSLNK`	`265 269`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`
`CONFLICT`	`554 554`		`R -> S (in Ref. 2; BAB64406).`

Sequence information

Length: 584 AA [This is the length of the unprocessed precursor]

Molecular weight: 65102 Da [This is the MW of the unprocessed precursor]

CRC64: 10492DE9D173C4E6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAVAPRVDG HVAPQRPEPT GHARKGSKAW LMMTTTDHKQ LGIMYIIMSF SFFFLGGLMA 

        70         80         90        100        110        120 
LLIRAELFTP GLQFLSNEQF NQLFTMHGTV MLLLYGTPIV WGFANYVLPL QIGAPDVAFP 

       130        140        150        160        170        180 
RLNAFGFWIT TVGGVAMLTG FLTPGGAADF GWTMYSPLSD AIHSPGLGSD MWIVGVGATG 

       190        200        210        220        230        240 
IGSVASAINM LTTILCLRAP GMTMFRMPIF TWNIFVVSVL ALLIFPLLLA AALGVLYDRK 

       250        260        270        280        290        300 
LGGHLYDPAN GGSLLWQHLF WFFGHPEVYV LALPFFGIVS EIIPVFSRKP MFGYVGLIFA 

       310        320        330        340        350        360 
TLSIGALSMA VWAHHMFVTG AVLLPFFSFM TFLISVPTGV KFFNWVGTMW KGHITWETPM 

       370        380        390        400        410        420 
IWSVGFMATF LFGGLTGIML ASPPLDFHLA DSYFLIAHFH YTLFGTVVFA SCAGVYFWFP 

       430        440        450        460        470        480 
KMTGRMMDER LGKIHFWLTF VGFHGTFLIQ HWVGNMGMPR RYADYLDSDG FTIYNQISTV 

       490        500        510        520        530        540 
FSFLLGLSVI PFIWNVFKSW RYGELVTVDD PWGYGNSLEW ATSCPPPRHN FASLPRIRSE 

       550        560        570        580 
RPAFELHYPH MIERMRAEAH TGHHDDINAP ELGTAPALAS DSSR

Q79VD7 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