ID   BIOW_CORPF              Reviewed;         243 AA.
AC   D8KN09;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 46.
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=cpfrc_01183;
OS   Corynebacterium pseudotuberculosis (strain FRC41).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=765874;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRC41;
RX   PubMed=21192786; DOI=10.1186/1471-2164-11-728;
RA   Trost E., Ott L., Schneider J., Schroder J., Jaenicke S., Goesmann A.,
RA   Husemann P., Stoye J., Dorella F.A., Rocha F.S., Soares Sde C.,
RA   D'Afonseca V., Miyoshi A., Ruiz J., Silva A., Azevedo V., Burkovski A.,
RA   Guiso N., Join-Lambert O.F., Kayal S., Tauch A.;
RT   "The complete genome sequence of Corynebacterium pseudotuberculosis FRC41
RT   isolated from a 12-year-old girl with necrotizing lymphadenitis reveals
RT   insights into gene-regulatory networks contributing to virulence.";
RL   BMC Genomics 11:728-728(2010).
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; CP002097; ADK28976.1; -; Genomic_DNA.
DR   RefSeq; WP_013242038.1; NC_014329.2.
DR   AlphaFoldDB; D8KN09; -.
DR   SMR; D8KN09; -.
DR   GeneID; 12299610; -.
DR   KEGG; cpu:CPFRC_05945; -.
DR   HOGENOM; CLU_076858_0_0_11; -.
DR   OMA; LCWSDDP; -.
DR   UniPathway; UPA00999; UER00351.
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..243
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412083"
SQ   SEQUENCE   243 AA;  26613 MW;  C6EEB9E0EF72E527 CRC64;
     MTFYSVRMRA SLQGQHISGA ETLVSCPTDV PRLTAQFVER AMNHAKGVPD AITTKIESIP
     ESDIQRVPRL LTREYQARDC HDAHGFVQQQ LTTVCSAEVA QKAVDLLLTI RNMRGAILLD
     AHSARRLEPD HNRGIRASNF GDASSISAKP DNKEIGISKN HYHEALILSS KVMSAPGIIA
     EICISDDPDY TTGYVSLNGV YTRVHTMKRL GSPLGGRVFI LDSEKASVAT AINHIENTPV
     LIL