ID   BIOW_SYNC1              Reviewed;         265 AA.
AC   Q3A3Z7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Pcar_1666;
OS   Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS   (Pelobacter carbinolicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Syntrophotaleaceae; Syntrophotalea.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL   Submitted (OCT-2005) 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; CP000142; ABA88910.1; -; Genomic_DNA.
DR   RefSeq; WP_011341400.1; NC_007498.2.
DR   AlphaFoldDB; Q3A3Z7; -.
DR   SMR; Q3A3Z7; -.
DR   STRING; 338963.Pcar_1666; -.
DR   EnsemblBacteria; ABA88910; ABA88910; Pcar_1666.
DR   KEGG; pca:Pcar_1666; -.
DR   eggNOG; COG1424; Bacteria.
DR   HOGENOM; CLU_076858_0_0_7; -.
DR   OMA; LCWSDDP; -.
DR   OrthoDB; 1268552at2; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000002534; 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;
KW   Reference proteome.
FT   CHAIN           1..265
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412087"
SQ   SEQUENCE   265 AA;  28886 MW;  953BDD4C577C5319 CRC64;
     MSESLYSIRM RSSCDERHIS GAENLAPAER LHALASAMVR RALAHDKGQA EQIFLSIEKV
     DTADIVCHGL PDIRTIRVAS VEQGRDAALS MLEKAGVNPQ AARRAMATMA RGAAPNGDSM
     RGAMLVDAST GQRLEKDRYR GVRVSRMDLD EQTSVRLKNL LQTAGLDNPH VREALVLAAK
     VIHAPGVIAE LCWSDDPGYT AGYVAGASLG YVRFPLLKPA GEVRGGRAFF LSSDADLAQL
     IPYLERQVVL IDRIGRIFPD ERWPA