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Q9CBQ5 (COX1_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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:
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:ML1728
OrganismMycobacterium leprae (strain TN) [Complete proteome] [HAMAP]
Taxonomic identifier272631 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceInferred 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.

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 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Probable cytochrome c oxidase subunit 1
PRO_0000183441

Regions

Transmembrane40 – 6021Helical; Potential
Transmembrane89 – 10921Helical; Potential
Transmembrane121 – 14121Helical; Potential
Transmembrane170 – 19021Helical; Potential
Transmembrane213 – 23321Helical; Potential
Transmembrane258 – 27821Helical; Potential
Transmembrane290 – 31021Helical; Potential
Transmembrane315 – 33521Helical; Potential
Transmembrane359 – 37921Helical; Potential
Transmembrane398 – 41821Helical; Potential
Transmembrane433 – 45321Helical; Potential
Transmembrane476 – 49621Helical; Potential

Sites

Metal binding861Iron (heme A axial ligand) By similarity
Metal binding2641Copper B By similarity
Metal binding2681Copper B By similarity
Metal binding3131Copper B By similarity
Metal binding3141Copper B By similarity
Metal binding3971Iron (heme A3 axial ligand) By similarity
Metal binding3991Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link264 ↔ 2681'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CBQ5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9CFE8C610E09F475

FASTA57463,957
        10         20         30         40         50         60 
MTAEALSSGE LKAIRPYPAR TGPKGNLVYK LITTTDHKMI GIMYCVACFI FFFVGGLLAL 

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

       130        140        150        160        170        180 
LNAFSFWLFL FGAAIGMAGF ITPGGAADFG WTAYTPLTDA IHSPGVGGDL WIMGLIVAGL 

       190        200        210        220        230        240 
GTILGAVNMI TTVVCLRAPG MTMFRMPIFT WNILVTSILV LIAFPLLTAA LFGLAADRHL 

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

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

       370        380        390        400        410        420 
FSVGFAVTFL LGGLTGVLLA SPPLDFHVTD SYFVVAHFHY VLFGTIVFST FAGIYFWFPK 

       430        440        450        460        470        480 
MTGRLLDEQL GKLHFWLTFI GFHTTFLVQH WLGDMGMPRR YADYLPTDGF QGLNVVSTIG 

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

       550        560        570 
PAFELHYPHM VERLRDEAYV GRRHAEELVE VSLH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL583923 Genomic DNA. Translation: CAC30681.1.
PIRB87125.
RefSeqNP_302190.1. NC_002677.1.

3D structure databases

ProteinModelPortalQ9CBQ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272631.ML1728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC30681; CAC30681; CAC30681.
GeneID910765.
KEGGmle:ML1728.
PATRIC18056644. VBIMycLep78757_3251.

Organism-specific databases

LepromaML1728.
CMRSearch...

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085275.
KOK02274.
OMAVNGAFGN.
OrthoDBEOG6B35XR.
ProtClustDBCLSK872133.

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_MYCLE
AccessionPrimary (citable) accession number: Q9CBQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 82 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