ID   BIOW_BACST              Reviewed;         258 AA.
AC   E8VHU4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 43.
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=BSn5_05960;
OS   Bacillus subtilis (strain BSn5).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=936156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSn5;
RX   PubMed=21317323; DOI=10.1128/jb.00129-11;
RA   Deng Y., Zhu Y., Wang P., Zhu L., Zheng J., Li R., Ruan L., Peng D.,
RA   Sun M.;
RT   "Complete genome sequence of Bacillus subtilis BSn5, an endophytic
RT   bacterium of Amorphophallus konjac with antimicrobial activity to plant
RT   pathogen Erwinia carotovora subsp. carotovora.";
RL   J. Bacteriol. 193:2070-2071(2011).
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; CP002468; ADV93820.1; -; Genomic_DNA.
DR   RefSeq; WP_015714551.1; NZ_VDQY01000004.1.
DR   AlphaFoldDB; E8VHU4; -.
DR   SMR; E8VHU4; -.
DR   KEGG; bsn:BSn5_05960; -.
DR   HOGENOM; CLU_076858_0_0_9; -.
DR   OMA; LCWSDDP; -.
DR   BioCyc; BSUB936156:BSN5_RS05895-MON; -.
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.
DR   TIGRFAMs; TIGR01204; bioW; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biotin biosynthesis; Ligase; Magnesium; Nucleotide-binding.
FT   CHAIN           1..258
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412080"
SQ   SEQUENCE   258 AA;  29527 MW;  550FCDD62E1931A2 CRC64;
     MQEETFYSVR MRASMNGSHE DGGKHISGGE RLIPFHEMKH TVNALLEKGL SHSRGKPDFM
     QIQFEEVYES IKTIQPLPVH TNEVSCPEEG QKLARLLLEK EGVSRDVIEK AYEQIPEWSD
     VRGAVLFDIH TGKRMDQTKE KGVRVSRMDW PDANFEKWAL HSHVPAHSRI KEALALASKV
     SWHPAAVAEL CWSDDPDYIT GYVAGKKMGY QRITAMKEYG TEEGCRVFFI DGSNDVNTYI
     HDLEKQPILI EWEEDHDS