ID   BIOW_METIM              Reviewed;         226 AA.
AC   D5VQA3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-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}; OrderedLocusNames=Metin_0084;
OS   Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=573063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11812 / JCM 15783 / ME;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT   "Complete sequence of Methanocaldococcus infernus ME.";
RL   Submitted (APR-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; CP002009; ADG12756.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5VQA3; -.
DR   SMR; D5VQA3; -.
DR   STRING; 573063.Metin_0084; -.
DR   EnsemblBacteria; ADG12756; ADG12756; Metin_0084.
DR   KEGG; mif:Metin_0084; -.
DR   eggNOG; arCOG05075; Archaea.
DR   HOGENOM; CLU_076858_0_0_2; -.
DR   OMA; LCWSDDP; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000002061; 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..226
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412095"
SQ   SEQUENCE   226 AA;  25531 MW;  8440E8A0220336CC CRC64;
     MRASREGKHI SGGERLVSEE KIEEAVLELL RKALTHENGK PDFINIKIEK IDKVNYIKAL
     PIKTITCKNK KEAREVAKKI LLEEGIPEEV VEKAFKIIDK GGMRGAAILN LNGERLEPDR
     ERGVRVKNID TSERLKEKIL KEGLGTERTV DAIAIASKVI RLGIIAELCT SDNKSYTTGY
     VATKKGYFRI TNLKNINEPG GRVFFVKDID EELIKRLEEE AYIIDL