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Q82AK9 (COX1A_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:SAV_6048
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces ›

Protein attributes

Sequence length579 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 – 579579Probable cytochrome c oxidase subunit 1-alpha
PRO_0000183450

Regions

Transmembrane44 – 6421Helical; Potential
Transmembrane93 – 11321Helical; Potential
Transmembrane125 – 14521Helical; Potential
Transmembrane174 – 19421Helical; Potential
Transmembrane217 – 23721Helical; Potential
Transmembrane262 – 28221Helical; Potential
Transmembrane295 – 31521Helical; Potential
Transmembrane319 – 33921Helical; Potential
Transmembrane363 – 38321Helical; Potential
Transmembrane397 – 41721Helical; 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
Q82AK9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 848C1E2D09B3589E

FASTA57963,950
        10         20         30         40         50         60 
MSILNEPQGA AAAEDSYENE LPVRRKQPGN VVVKWLTTTD HKTIGTLYLV TSFAFFCIGG 

        70         80         90        100        110        120 
VMALLMRAEL ARPGMQIMSS EQFNQAFTMH GTIMLLMFAT PLFAGFANWI MPLQIGAPDV 

       130        140        150        160        170        180 
AFPRLNMFAY WLYLFGSLIA VGGFLTPQGA ADFGWFAYSP LSDAVRSPGI GADMWIMGLA 

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

       250        260        270        280        290        300 
DRKFGAHVFD AANGGALLWQ HLFWFFGHPE VYIIALPFFG IISEVIPVFS RKPMFGYMGL 

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

       370        380        390        400        410        420 
TPMLWATGFL ITFTFGGLTG VILASPPMDF HVSDSYFVVA HFHYVVFGTV VFAMFSGFHY 

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

       490        500        510        520        530        540 
STICSFLLGL SILPFLYNVW KTAKYGKPVG VDDPWGYGRS LEWATSCPPP RHNFLTLPRI 

       550        560        570 
RSESPAFDLH HPEIAALDQL ENAGHGEKAA VAGGKEAGK

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000030 Genomic DNA. Translation: BAC73759.1.
RefSeqNP_827224.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82AK9.
ModBaseSearch...

Protein-protein interaction databases

STRING227882.SAV_6048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC73759; BAC73759; SAV_6048.
GeneID1211382.
KEGGsma:SAV_6048.
PATRIC23726122. VBIStrAve112782_6414.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
KOK02274.
OMAFLIGGIM.
ProtClustDBCLSK2519270.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-6128-MONOMER.
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. COX1. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1A_STRAW
AccessionPrimary (citable) accession number: Q82AK9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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