ID   BIOW_BACA1              Reviewed;         258 AA.
AC   E3E2E2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 54.
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};
GN   OrderedLocusNames=BATR1942_12910;
OS   Bacillus atrophaeus (strain 1942).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=720555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1942;
RA   Gibbons H.S., Broomall S., McNew L.A., Daligault H., Chapman C., Bruce D.,
RA   Karavis M., McGregor P., Hong C., Park K.H., Akmal A., Feldman A.,
RA   Lin J.S., Chang W.E., Higgs B.W., Demirev P., Lindquist J., Liem A.,
RA   Fochler E., Tapia R., Bishop-Lilly K., Detter C., Han C., Sozhamannan S.,
RA   Rosenzweig C.N., Skowronski E.;
RT   "Genomic signatures of strain selection and enhancement in Bacillus
RT   atrophaeus subsp. Globigii, a historical biowarfare simulant.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002207; ADP33509.1; -; Genomic_DNA.
DR   RefSeq; WP_013390629.1; NC_014639.1.
DR   AlphaFoldDB; E3E2E2; -.
DR   SMR; E3E2E2; -.
DR   STRING; 720555.BATR1942_12910; -.
DR   EnsemblBacteria; ADP33509; ADP33509; BATR1942_12910.
DR   GeneID; 23411018; -.
DR   KEGG; bae:BATR1942_12910; -.
DR   eggNOG; COG1424; Bacteria.
DR   HOGENOM; CLU_076858_0_0_9; -.
DR   OMA; LCWSDDP; -.
DR   OrthoDB; 1268552at2; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000006867; 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.
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_0000412077"
SQ   SEQUENCE   258 AA;  29877 MW;  2C007CCA6BC21A5F CRC64;
     MREEKFYSVR MRASKNGSHE VGGKHLSGGE RLTTYENMIH TVNALLEKGI YHSRGKPDFM
     KIQFECIDEP IQLVNPLHIE THEVESAEKG QVLARKLLEK AGIQKKMIDL AYEQIPECSG
     LRGAILFDIH SGKRIDQRKE RGVRVSRMDW PDTNFDKWTK CYQMPRNSRI KEALVLATKV
     SEHPATIAEL CWSDDPDYIT GYVASKKLGY QRITKLKEYG NESGCRIFFV DGLRDLETYI
     DYLEKQPVFI QWEEENDA