Cytochrome c oxidase subunit 1 - Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)

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Q79VD7 (COX1_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. 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 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:	Cgl2523, cg2780

Organism

Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]

Taxonomic identifier

196627 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length	584 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 By similarity.
Catalytic activity	4 ferrocytochrome c + O₂ + 4 H⁺ = 4 ferricytochrome c + 2 H₂O.
Cofactor	Binds 1 copper B per subunit By similarity. Binds 2 heme groups per subunit By similarity.
Pathway	Energy metabolism; oxidative phosphorylation.
Subunit structure	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). Ref.2
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the heme-copper respiratory oxidase family.
Mass spectrometry	Molecular mass is 64955.8±164.1 Da from positions 1 - 584. Determined by MALDI. Ref.2

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 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 – 584

584

Cytochrome c oxidase subunit 1

PRO_0000183440

Regions

Transmembrane

43 – 63

Helical; Potential

Transmembrane

90 – 110

Helical; Potential

Transmembrane

122 – 142

Helical; Potential

Transmembrane

171 – 191

Helical; Potential

Transmembrane

214 – 234

Helical; Potential

Transmembrane

259 – 279

Helical; Potential

Transmembrane

292 – 312

Helical; Potential

Transmembrane

316 – 336

Helical; Potential

Transmembrane

360 – 380

Helical; Potential

Transmembrane

399 – 419

Helical; Potential

Transmembrane

434 – 454

Helical; Potential

Transmembrane

477 – 497

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

265

Copper B Probable

Metal binding

269

Copper B Probable

Metal binding

314

Copper B Probable

Metal binding

315

Copper B Probable

Metal binding

398

Iron (heme A3 axial ligand) Probable

Metal binding

400

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

265 ↔ 269

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

Experimental info

Sequence conflict

554

R → S in BAB64406. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q79VD7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 10492DE9D173C4E6
Show »

FASTA

584

65,102

        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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium glutamicum respiratory chain containing an unusual diheme cytochrome c1." Niebisch A., Bott M. Arch. Microbiol. 175:282-294(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]	"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." Sakamoto J., Shibata T., Mine T., Miyahara R., Torigoe T., Noguchi S., Matsushita K., Sone N. Microbiology 147:2865-2871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, HEME CHARACTERIZATION, MASS SPECTROMETRY. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes." Ikeda M., Nakagawa S. Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." 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. Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[5]	"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." Niebisch A., Bott M. J. Biol. Chem. 278:4339-4346(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DETECTION IN A SUPERCOMPLEX WITH MENAQUINOL-CYTOCHROME C REDUCTASE (CYTOCHROME BC1). Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ306417 Genomic DNA. Translation: CAC33824.1. AB052748 Genomic DNA. Translation: BAB64406.1. BA000036 Genomic DNA. Translation: BAB99916.1. BX927155 Genomic DNA. Translation: CAF21186.1.
RefSeq	NP_601724.2. NC_003450.3. YP_226765.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q79VD7.
ModBase	Search...
Protein-protein interaction databases
STRING	196627.cg2780.
Protein family/group databases
TCDB	3.D.4.4.2. proton-translocating cytochrome oxidase (COX) superfamily.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB99916; BAB99916; BAB99916. CAF21186; CAF21186; cg2780.
GeneID	1020472. 3344025.
KEGG	cgb:cg2780. cgl:NCgl2437.
PATRIC	21497064. VBICorGlu203724_2457.
Phylogenomic databases
eggNOG	COG0843.
HOGENOM	HOG000085274.
KO	K02274.
OMA	FGASLEW.
ProtClustDB	CLSK2519649.
Enzyme and pathway databases
BioCyc	CGLU196627:GJDM-2503-MONOMER.
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_CORGL

Accession

Primary (citable) accession number: Q79VD7
Secondary accession number(s): Q93HZ5, Q9AEL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 81 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents