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Q79VD7 (COX1_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 584584Cytochrome c oxidase subunit 1
PRO_0000183440

Regions

Transmembrane43 – 6321Helical; Potential
Transmembrane90 – 11021Helical; Potential
Transmembrane122 – 14221Helical; Potential
Transmembrane171 – 19121Helical; Potential
Transmembrane214 – 23421Helical; Potential
Transmembrane259 – 27921Helical; Potential
Transmembrane292 – 31221Helical; Potential
Transmembrane316 – 33621Helical; Potential
Transmembrane360 – 38021Helical; Potential
Transmembrane399 – 41921Helical; Potential
Transmembrane434 – 45421Helical; Potential
Transmembrane477 – 49721Helical; Potential

Sites

Metal binding871Iron (heme A axial ligand) Probable
Metal binding2651Copper B Probable
Metal binding2691Copper B Probable
Metal binding3141Copper B Probable
Metal binding3151Copper B Probable
Metal binding3981Iron (heme A3 axial ligand) Probable
Metal binding4001Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link265 ↔ 2691'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Sequence conflict5541R → S in BAB64406. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q79VD7 [UniParc].

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

FASTA58465,102
        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' 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. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., 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.
RefSeqNP_601724.2. NC_003450.3.
YP_226765.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ79VD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2780.

Protein family/group databases

TCDB3.D.4.4.2. the proton-translocating cytochrome oxidase (cox) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99916; BAB99916; BAB99916.
CAF21186; CAF21186; cg2780.
GeneID1020472.
KEGGcgb:cg2780.
cgl:NCgl2437.
PATRIC21497064. VBICorGlu203724_2457.

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
KOK02274.
OMAISETVCA.
OrthoDBEOG6B35XR.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_CORGL
AccessionPrimary (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: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways