ID   BIOW_PERMH              Reviewed;         247 AA.
AC   C0QSH0;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=PERMA_1854;
OS   Persephonella marina (strain DSM 14350 / EX-H1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella.
OX   NCBI_TaxID=123214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14350 / EX-H1;
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}.
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DR   EMBL; CP001230; ACO03122.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0QSH0; -.
DR   SMR; C0QSH0; -.
DR   STRING; 123214.PERMA_1854; -.
DR   PRIDE; C0QSH0; -.
DR   EnsemblBacteria; ACO03122; ACO03122; PERMA_1854.
DR   KEGG; pmx:PERMA_1854; -.
DR   eggNOG; COG1424; Bacteria.
DR   HOGENOM; CLU_076858_0_0_0; -.
DR   OMA; LCWSDDP; -.
DR   UniPathway; UPA00999; UER00351.
DR   Proteomes; UP000001366; 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..247
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000412088"
SQ   SEQUENCE   247 AA;  28403 MW;  D07580CFB0D8F70C CRC64;
     MYYSIKLRAS RDGKHLSGGE RIVLKDKIEE AVNQLYRKAE PKDPDEINIK IESIKEKPLV
     IKSSLKIENI ICEDYKSSNQ IALEILKRST GIPVERLKEL IDLVHTGSAP DGSNMRGAMI
     VNQKGERIEL DHFRGIRTTT VDFLDRDKIL KKLVKKGYTE RTVDALCLTT KNMLYPDMIA
     EYCISDEPDY ITGYVSTKDF YYRITPLKSE GNPKGGRIYF VRNSIDLQDF YRFLQEKPVL
     IEDVGID