ID   BIOW_METSF              Reviewed;         233 AA.
AC   D3S7P2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 49.
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=MFS40622_0356;
OS   Methanocaldococcus sp. (strain FS406-22).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus; unclassified Methanocaldococcus.
OX   NCBI_TaxID=644281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FS406-22;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Leigh J.,
RA   Whitman W.B., Woyke T.;
RT   "Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.";
RL   Submitted (FEB-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; CP001901; ADC69052.1; -; Genomic_DNA.
DR   RefSeq; WP_012979963.1; NC_013887.1.
DR   AlphaFoldDB; D3S7P2; -.
DR   SMR; D3S7P2; -.
DR   STRING; 644281.MFS40622_0356; -.
DR   PRIDE; D3S7P2; -.
DR   EnsemblBacteria; ADC69052; ADC69052; MFS40622_0356.
DR   GeneID; 8804195; -.
DR   KEGG; mfs:MFS40622_0356; -.
DR   eggNOG; arCOG05075; Archaea.
DR   HOGENOM; CLU_076858_0_0_2; -.
DR   OMA; LCWSDDP; -.
DR   OrthoDB; 68002at2157; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000002189; 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..233
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412096"
SQ   SEQUENCE   233 AA;  26564 MW;  3C435988EF25C885 CRC64;
     MYSIKMRASK NGKHISGAER IVNKDEIEDV ARELIKRALT HENGTPDFIN IKIEEIKEDI
     EYIDHLPIKT IHCKNKEEAR EKAREILRNE GIPDKVIDYA YEIIDKGGMR GAAILNLKGE
     RLEPDKERGV RVKNIDTTKE LKEKILKEKL GTERTVDAIA IASKVIHLGV IAELCTSDNK
     SYTTGYVATK RGYFRITNLK KEGESGGRVF FVKNDVNIED LIDKLENKPF IIK