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Q9X813 (COX1A_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:
Probable cytochrome c oxidase subunit 1-alpha

EC=1.9.3.1
Alternative name(s):
Cytochrome aa3 subunit 1-alpha
Cytochrome c oxidase polypeptide I-alpha
Gene names
Name:ctaD1
Ordered Locus Names:SCO2155
ORF Names:SC6G10.28c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length578 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 – 578578Probable cytochrome c oxidase subunit 1-alpha
PRO_0000183452

Regions

Transmembrane44 – 6421Helical; Potential
Transmembrane93 – 11321Helical; Potential
Transmembrane125 – 14521Helical; Potential
Transmembrane174 – 19421Helical; Potential
Transmembrane217 – 23721Helical; Potential
Transmembrane262 – 28221Helical; Potential
Transmembrane294 – 31421Helical; Potential
Transmembrane319 – 33921Helical; Potential
Transmembrane363 – 38321Helical; Potential
Transmembrane402 – 42221Helical; Potential
Transmembrane437 – 45721Helical; Potential
Transmembrane480 – 50021Helical; Potential

Sites

Metal binding901Iron (heme A axial ligand) By similarity
Metal binding2681Copper B By similarity
Metal binding2721Copper B By similarity
Metal binding3171Copper B By similarity
Metal binding3181Copper B By similarity
Metal binding4011Iron (heme A3 axial ligand) By similarity
Metal binding4031Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link268 ↔ 2721'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X813 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 2A25FF2A913DC461

FASTA57864,122
        10         20         30         40         50         60 
MSILNEPQGA SAAEDSYENE LPVRRKQPGN VVIKWLTTTD HKTIGTMYLV TSFAFFVIGG 

        70         80         90        100        110        120 
VMALFMRAEL ARPGLQIMSN EQFNQAFTMH GTIMLLMFAT PLFAGFANWI MPLQIGAPDV 

       130        140        150        160        170        180 
AFPRLNMFAY WLYLFGSTIA VGGFLTPQGA ADFGWFAYSP LSDAVHSPGI GGDLWIMGLA 

       190        200        210        220        230        240 
FSGFGTILGS VNFITTIICM RAPGMTMFRM PIFTWNVLLT GVLVLLAFPV LAAALFALEA 

       250        260        270        280        290        300 
DRKFGAHIFD SSNGGALLWQ HLFWFFGHPE VYIIALPFFG IVSEIIPVFS RKPIFGYMGL 

       310        320        330        340        350        360 
IGATIAIAGL SVTVWAHHMY VTGGVLLPFF SFMTFLIAVP TGVKFFNWIG TMWKGSLSFE 

       370        380        390        400        410        420 
TPMLWSTGFL ITFLFGGLTG VILASPPLDF HVSDSYFVVA HFHYVVFGTV VFAMFAGFHF 

       430        440        450        460        470        480 
WWPKFTGKML DERLGKITFW TLFVGFHGTF LVQHWLGAEG MPRRYADYLA ADGFTALNTI 

       490        500        510        520        530        540 
STISSFLLGM SILPFFYNIW KTAKYGKKIE VDDPWGYGRS LEWATSCPPP RHNFLTLPRI 

       550        560        570 
RSESPAFDLH HPEISAIDQL ENVGHGEKAL AGGKEAGK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939111 Genomic DNA. Translation: CAB39882.1.
PIRT35537.
RefSeqNP_626411.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9X813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO2155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB39882; CAB39882; CAB39882.
GeneID1097589.
KEGGsco:SCO2155.
PATRIC23733962. VBIStrCoe124346_2190.

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
KOK02274.
OMAVNAIGFW.
OrthoDBEOG6B35XR.
PhylomeDBQ9X813.
ProtClustDBCLSK2519270.

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 nameCOX1A_STRCO
AccessionPrimary (citable) accession number: Q9X813
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1999
Last modified: April 16, 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