ID   BIOW_THEAH              Reviewed;         243 AA.
AC   D3SN37;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=Thal_1538;
OS   Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX   NCBI_TaxID=638303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14484 / JCM 11386 / HI 11/12;
RX   DOI=10.4056/sigs.761490;
RA   Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA   Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA   Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T).";
RL   Stand. Genomic Sci. 2:194-202(2010).
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; CP001931; ADC90167.1; -; Genomic_DNA.
DR   RefSeq; WP_012992573.1; NC_013894.1.
DR   AlphaFoldDB; D3SN37; -.
DR   SMR; D3SN37; -.
DR   STRING; 638303.Thal_1538; -.
DR   EnsemblBacteria; ADC90167; ADC90167; Thal_1538.
DR   KEGG; tal:Thal_1538; -.
DR   eggNOG; COG1424; Bacteria.
DR   HOGENOM; CLU_076858_0_0_0; -.
DR   OMA; LCWSDDP; -.
DR   OrthoDB; 1268552at2; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000002043; 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..243
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412091"
SQ   SEQUENCE   243 AA;  27794 MW;  41A8A7090D0804F2 CRC64;
     MRSIRMRAEF QGEHVSGAER IVPYHEVEKT VLELLKRPRV YDKVVITVER LKDVEIVPKA
     LPILSYDFKS VEEARAFAVS KLVEAGVPKP VAELAIKLLH EGPNPKGGNM RGAVLMDVET
     GERLEPDRER GIRTTRMDWK DRKYIKEVLK KRGIKREYLE RLIDALAVAT KNVYCGVLAE
     LCWSDDPEYT TGYVAGPHIG YVRIKPMKEE GVPIGGRVYF IRKENLEKII QCLQEKPILI
     NNL