ID   BIOW_STAAE              Reviewed;         230 AA.
AC   A6QJR2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=6-carboxyhexanoate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_00668};
DE            EC=6.2.1.14 {ECO:0000255|HAMAP-Rule:MF_00668};
DE   AltName: Full=Pimeloyl-CoA synthase {ECO:0000255|HAMAP-Rule:MF_00668};
GN   Name=bioW {ECO:0000255|HAMAP-Rule:MF_00668}; OrderedLocusNames=NWMN_2322;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
CC   -!- FUNCTION: Catalyzes the transformation of pimelate into pimeloyl-CoA
CC       with concomitant hydrolysis of ATP to AMP. {ECO:0000255|HAMAP-
CC       Rule:MF_00668}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:14781, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:36165, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57360, ChEBI:CHEBI:456215; EC=6.2.1.14;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00668};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00668};
CC   -!- PATHWAY: Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis;
CC       pimeloyl-CoA from pimelate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00668}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00668}.
CC   -!- SIMILARITY: Belongs to the BioW family. {ECO:0000255|HAMAP-
CC       Rule:MF_00668}.
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DR   EMBL; AP009351; BAF68594.1; -; Genomic_DNA.
DR   RefSeq; WP_000286875.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QJR2; -.
DR   SMR; A6QJR2; -.
DR   EnsemblBacteria; BAF68594; BAF68594; NWMN_2322.
DR   KEGG; sae:NWMN_2322; -.
DR   HOGENOM; CLU_076858_0_0_9; -.
DR   OMA; LCWSDDP; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000006386; Chromosome.
DR   GO; GO:0042410; F:6-carboxyhexanoate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00668; BioW; 1.
DR   InterPro; IPR005499; BioW.
DR   Pfam; PF03744; BioW; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biotin biosynthesis; Ligase; Magnesium; Nucleotide-binding.
FT   CHAIN           1..230
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_1000072718"
SQ   SEQUENCE   230 AA;  26092 MW;  345AB71E281355DE CRC64;
     MYSIKMRSSN QDVHISGAET ICEFDKIEQT VQRFYNKGFF HENGQPDFLN IKIQKIMEPI
     QQIKALQIIE DDKANLQHLT QECGVTEQAL NQGMTYIKNE TVYTGAIILS AISGKRLDSF
     GQRGIRATHF SFEDINNKGD LNERVTDALA IASCINAHPY VKGELCVSDD LTYTTGYFAA
     AKIGYHRLFD IKPVNTRYGG RIIFVDDCID LNHYISFLES TPKQVVYETV