ID   BIOW_SULAA              Reviewed;         245 AA.
AC   C1DW75;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=SULAZ_1395;
OS   Sulfurihydrogenibium azorense (strain Az-Fu1 / DSM 15241 / OCM 825).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium.
OX   NCBI_TaxID=204536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Az-Fu1 / DSM 15241 / OCM 825;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001229; ACN98309.1; -; Genomic_DNA.
DR   RefSeq; WP_012673634.1; NC_012438.1.
DR   AlphaFoldDB; C1DW75; -.
DR   SMR; C1DW75; -.
DR   STRING; 204536.SULAZ_1395; -.
DR   EnsemblBacteria; ACN98309; ACN98309; SULAZ_1395.
DR   KEGG; saf:SULAZ_1395; -.
DR   eggNOG; COG1424; Bacteria.
DR   HOGENOM; CLU_076858_0_0_0; -.
DR   OMA; LCWSDDP; -.
DR   OrthoDB; 1268552at2; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000001369; 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..245
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412089"
SQ   SEQUENCE   245 AA;  27940 MW;  6A4A75479A9D78EF CRC64;
     MKEYFSVKMR ASLQGRHVSG AERIVLKEDL PTVISQLSQR PKEYDSLNIK VEKINDLNYI
     EKSLNVKTIN VKDWIEGNKV AVEILQNQGV DKKIAEKYIN LIHQGAVNGE NMRGAMIVNL
     SGERVEKDKT RGIRTVNIDF EDRKAITELL KEKGYTERTV DALALATKTL NHPDIVAEYC
     ISDDPSYTTG YVATKTTYYR INPLKQLSNE KGGRIYFVKD TANIEDIYQY LESEAFLIKQ
     LGDLQ