ID   BIOW_BACAS              Reviewed;         256 AA.
AC   E1UV19;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 51.
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=BAMF_1924;
OS   Bacillus amyloliquefaciens (strain ATCC 23350 / DSM 7 / BCRC 11601 / CCUG
OS   28519 / NBRC 15535 / NRRL B-14393 / F).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=692420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / CCUG 28519 / NBRC 15535 / NRRL
RC   B-14393 / F;
RX   PubMed=21262282; DOI=10.1016/j.jbiotec.2011.01.006;
RA   Ruckert C., Blom J., Chen X., Reva O., Borriss R.;
RT   "Genome sequence of B. amyloliquefaciens type strain DSM7(T) reveals
RT   differences to plant-associated B. amyloliquefaciens FZB42.";
RL   J. Biotechnol. 155:78-85(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; FN597644; CBI43050.1; -; Genomic_DNA.
DR   RefSeq; WP_013352461.1; NC_014551.1.
DR   AlphaFoldDB; E1UV19; -.
DR   SMR; E1UV19; -.
DR   KEGG; bao:BAMF_1924; -.
DR   HOGENOM; CLU_076858_0_0_9; -.
DR   OMA; LCWSDDP; -.
DR   BioCyc; BAMY692420:BAMF_RS30275-MON; -.
DR   BRENDA; 6.2.1.14; 630.
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..256
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412075"
SQ   SEQUENCE   256 AA;  28861 MW;  A26CD57FD3066E58 CRC64;
     MEEEIYYSVR MRASRDAPHE QGGKHISGGE RLITYSGLQE AVNGLLHKGF SHSRGTPDFM
     QIQLESINQP IKTIRPLPVA VHQTDTAEKG QAVARKLLQK AGIPPHMIEK AYQNIAEYAE
     VRGAVLFDIQ TGKRIDGRKE RGVRVSRMDW PAHDFQKWTL EHKMPENPRI KEAHAIAAKV
     CAHPGIIAEL CWSDDPDYIT GYVAAKKLGY QRITKMKNAG DESGCRIFFT DGAIDTESCI
     HFLEKQPVFI QREGKI