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Q2FVJ9 (BIOW_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. 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:
6-carboxyhexanoate--CoA ligase

EC=6.2.1.14
Alternative name(s):
Pimeloyl-CoA synthase
Gene names
Name:bioW
Ordered Locus Names:SAOUHSC_02712
OrganismStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP By similarity. HAMAP MF_00668

Catalytic activity

ATP + 6-carboxyhexanoate + CoA = AMP + diphosphate + 6-carboxyhexanoyl-CoA. HAMAP MF_00668

Cofactor

Magnesium By similarity. HAMAP MF_00668

Pathway

Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis; pimeloyl-CoA from pimelate: step 1/1. HAMAP MF_00668

Subunit structure

Homodimer By similarity. HAMAP MF_00668

Sequence similarities

Belongs to the BioW family.

Ontologies

Keywords
   Biological processBiotin biosynthesis
   LigandATP-binding
Magnesium
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processbiotin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function6-carboxyhexanoate-CoA ligase activity

Inferred from electronic annotation. Source: EC

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2302306-carboxyhexanoate--CoA ligase HAMAP MF_00668
PRO_1000044697

Sequences

Sequence LengthMass (Da)Tools
Q2FVJ9 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 345AB71E281355DE

FASTA23026,092
        10         20         30         40         50         60 
MYSIKMRSSN QDVHISGAET ICEFDKIEQT VQRFYNKGFF HENGQPDFLN IKIQKIMEPI 

        70         80         90        100        110        120 
QQIKALQIIE DDKANLQHLT QECGVTEQAL NQGMTYIKNE TVYTGAIILS AISGKRLDSF 

       130        140        150        160        170        180 
GQRGIRATHF SFEDINNKGD LNERVTDALA IASCINAHPY VKGELCVSDD LTYTTGYFAA 

       190        200        210        220        230 
AKIGYHRLFD IKPVNTRYGG RIIFVDDCID LNHYISFLES TPKQVVYETV 

« Hide

References

[1]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000253 Genomic DNA. Translation: ABD31720.1.
RefSeqYP_501174.1. NC_007795.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2FVJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000028926; EBSTAP00000027877; EBSTAG00000028924.
GeneID3919731.
GenomeReviewsGene locus SAOUHSC_02712 in contig CP000253_GR.
KEGGsao:SAOUHSC_02712.
PATRIC19582701. VBIStaAur99865_2456.

Phylogenomic databases

eggNOGCOG1424.
GeneTreeEBGT00050000025018.
HOGENOMHBG507782.
OMATTGYVAT.
ProtClustDBPRK01322.

Enzyme and pathway databases

BioCycSAUR93061:SAOUHSC_02712-MONOMER.

Family and domain databases

HAMAPMF_00668. BioW.
[Tree]
InterProIPR005499. BioW.
[Graphical view]
KOK01906.
PfamPF03744. BioW. 1 hit.
[Graphical view]
ProDomPD017229. BioW. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameBIOW_STAA8
AccessionPrimary (citable) accession number: Q2FVJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 21, 2006
Last modified: January 25, 2012
This is version 32 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