ID   BIOW_VEIPT              Reviewed;         242 AA.
AC   D1BMT0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=Vpar_1006;
OS   Veillonella parvula (strain ATCC 10790 / DSM 2008 / CCUG 5123 / JCM 12972 /
OS   NCTC 11810 / Te3) (Veillonella alcalescens).
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=479436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10790 / DSM 2008 / CCUG 5123 / JCM 12972 / NCTC 11810 / Te3;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P., Woyke T.,
RA   Wu D., Wellnitz S., Schneider S., Gronow S., Klenk H.P., Eisen J.A.;
RT   "The complete genome of Veillonella parvula DSM 2008.";
RL   Submitted (NOV-2009) 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; CP001820; ACZ24687.1; -; Genomic_DNA.
DR   RefSeq; WP_012864431.1; NC_013520.1.
DR   AlphaFoldDB; D1BMT0; -.
DR   SMR; D1BMT0; -.
DR   STRING; 479436.Vpar_1006; -.
DR   EnsemblBacteria; ACZ24687; ACZ24687; Vpar_1006.
DR   KEGG; vpr:Vpar_1006; -.
DR   PATRIC; fig|479436.6.peg.982; -.
DR   eggNOG; COG1424; Bacteria.
DR   HOGENOM; CLU_076858_0_0_9; -.
DR   OMA; LCWSDDP; -.
DR   OrthoDB; 1268552at2; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000007968; 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..242
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412093"
SQ   SEQUENCE   242 AA;  26544 MW;  5C40D0021350CF0F CRC64;
     MDELYSVRMR AAQGGPHENG GHHISGAERI VTLNQVGFIA QSLAERALHH SKGTADFINI
     TVDLIPSETI TYIDCLKVKE HTANTVTEAH QLAVKLLQGT DISESAIRNS IFLLKSLVSS
     MRGAMLVDAI SGERLDAGNR GVRVSHMDSF DSDKLGDNEH MREALVLASK VQSAEGIVGE
     LCWSDDPDYT IGYVACNGVY HRIPNMKEIG SNLGGRVFFV KPNIDLEGVI EYLEKEPVLV
     QW