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Q828X4 (COX1B_STRAW) 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:
Putative cytochrome c oxidase subunit 1-beta

EC=1.9.3.1
Alternative name(s):
Cytochrome aa3 subunit 1-beta
Cytochrome c oxidase polypeptide I-beta
Gene names
Name:ctaD2
Ordered Locus Names:SAV_6537
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length563 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 – 563563Putative cytochrome c oxidase subunit 1-beta
PRO_0000183451

Regions

Transmembrane34 – 5421Helical; Potential
Transmembrane76 – 9621Helical; Potential
Transmembrane117 – 13721Helical; Potential
Transmembrane164 – 18421Helical; Potential
Transmembrane208 – 22821Helical; Potential
Transmembrane252 – 27221Helical; Potential
Transmembrane284 – 30421Helical; Potential
Transmembrane309 – 32921Helical; Potential
Transmembrane353 – 37321Helical; Potential
Transmembrane392 – 41221Helical; Potential
Transmembrane427 – 44721Helical; Potential
Transmembrane470 – 49021Helical; Potential

Sites

Metal binding801Iron (heme A axial ligand) By similarity
Metal binding2581Copper B By similarity
Metal binding2621Copper B By similarity
Metal binding3071Copper B By similarity
Metal binding3081Copper B By similarity
Metal binding3911Iron (heme A3 axial ligand) By similarity
Metal binding3931Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link258 ↔ 2621'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q828X4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: DE106F5AFBEBC7E1

FASTA56362,439
        10         20         30         40         50         60 
MGTDTAQATA RPVRTQQPGR LIVDWLTTTD HKKIGHLYLI TSFAFFLIGG VMALVMRAEL 

        70         80         90        100        110        120 
ARPGMQIVDN NQFNQLFTLH GTIMLLLFAT PTFAGFANEI MPLQIGSPDV AFPRLNMLSY 

       130        140        150        160        170        180 
WLFLFGGLIV LGSLAVPSGP AAFGWFAYAP LNSLERSPGI GADMWIMGLA LAGFGTILGS 

       190        200        210        220        230        240 
VNFLTTIIGM RAPGMTMFRM PIFTWNTLFT SILVLMAFPV LAAALLVLEA DRRFGSQVFD 

       250        260        270        280        290        300 
AANGGALLWQ HLFWFFGHPE VYIIALPFFG IITEIIPVFS RKPIFGYLTL IGATAAITGL 

       310        320        330        340        350        360 
SVVVWAHHMF ATGAVLLPFF SFMSFLIAVP TGVKFFNWTG TMLKGSLSFE TPMLWATGFL 

       370        380        390        400        410        420 
VSFLFGGLTG VILASPPLDF HVTDSYFVVA HFHYVVFGTV VFATFGGFYF WWPKFTGKML 

       430        440        450        460        470        480 
DERLGKIHFW TLFVGFHTTF LVQHWLGAEG MPRRYADYLA ADGFTALNTL STIGAFLLGM 

       490        500        510        520        530        540 
STLPFLYNVW KTARYGRKVE VDDPWGFGRS LEWTTSCPPP RHNFVTLPRV RSESPAFDLH 

       550        560 
HPAHAGEAPQ PEPKHEQADR EPS 

« 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: BAC74248.1.
RefSeqNP_827713.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ828X4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_6537.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC74248; BAC74248; SAV_6537.
GeneID1216877.
KEGGsma:SAV_6537.
PATRIC23727168. VBIStrAve112782_6933.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085275.
KOK02274.
OMAFADGHYW.
OrthoDBEOG6B35XR.
ProtClustDBCLSK2757993.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-6622-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. SSF81442. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1B_STRAW
AccessionPrimary (citable) accession number: Q828X4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2003
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