ID   BIOW_BACAM              Reviewed;         290 AA.
AC   Q70JY7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 42.
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};
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FZB42;
RX   PubMed=14762003; DOI=10.1128/jb.186.4.1084-1096.2004;
RA   Koumoutsi A., Chen X.H., Henne A., Liesegang H., Hitzeroth G., Franke P.,
RA   Vater J., Borriss R.;
RT   "Structural and functional characterization of gene clusters directing
RT   nonribosomal synthesis of bioactive cyclic lipopeptides in Bacillus
RT   amyloliquefaciens strain FZB42.";
RL   J. Bacteriol. 186:1084-1096(2004).
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; AJ576102; CAE11261.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q70JY7; -.
DR   SMR; Q70JY7; -.
DR   eggNOG; COG1424; Bacteria.
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..290
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412074"
SQ   SEQUENCE   290 AA;  32634 MW;  F55D13142466EB63 CRC64;
     MTYSEKALIF CISVNLKFIL VHINFQSKRK EGNICGKKPT YSVRMRASRN APHEQGGKHI
     SGGERLITYS GLQEAVDGLL HKGFSHSRGI PDFMQIQLES INEPIETIRP LPVAFHQSDT
     PEKGQAIARK LLQKAGIPPH MIEKAYENIA EYAEARGAVL FDIRAGERID GRGNRGVRVS
     RMDWPSHDFQ KWAFTHNMPE NSRIKEAHAI AAKVCAHPGI IAELCWSDDP DYITGYVAAK
     KLGYQRIAKM KNAGDESGCR IFFTDGSIDT ESCIHFLEKQ PVFIQREENI