ID   BIOW_LYSSH              Reviewed;         245 AA.
AC   P22822;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=6-carboxyhexanoate--CoA ligase;
DE            EC=6.2.1.14;
DE   AltName: Full=Pimeloyl-CoA synthase;
GN   Name=bioW;
OS   Lysinibacillus sphaericus (Bacillus sphaericus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10208 / DSM 5019 / NBRC 3525 / NCIMB 11935 / NRS 966 / 1911;
RX   PubMed=2110099; DOI=10.1016/0378-1119(90)90496-e;
RA   Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M.,
RA   Villeval D., Kisou T., Kamogawa K., Lemoine Y.;
RT   "Cloning and characterization of the Bacillus sphaericus genes controlling
RT   the bioconversion of pimelate into dethiobiotin.";
RL   Gene 87:63-70(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15, FUNCTION AS A PIMELOYL-COA SYNTHASE, CATALYTIC
RP   ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC 10208 / DSM 5019 / NBRC 3525 / NCIMB 11935 / NRS 966 / 1911;
RX   PubMed=1445232; DOI=10.1042/bj2870685;
RA   Ploux O., Soularue P., Marquet A., Gloeckler R., Lemoine Y.;
RT   "Investigation of the first step of biotin biosynthesis in Bacillus
RT   sphaericus. Purification and characterization of the pimeloyl-CoA synthase,
RT   and uptake of pimelate.";
RL   Biochem. J. 287:685-690(1992).
CC   -!- FUNCTION: Catalyzes the transformation of pimelate into pimeloyl-CoA
CC       with concomitant hydrolysis of ATP to AMP.
CC       {ECO:0000269|PubMed:1445232}.
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:0000269|PubMed:1445232};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by magnesium above 10 mM and metal
CC       chelators such as 1, 10-phenanthroline and EDTA.
CC       {ECO:0000269|PubMed:1445232}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=33 uM for CoASH {ECO:0000269|PubMed:1445232};
CC         KM=145 uM for pimelate {ECO:0000269|PubMed:1445232};
CC         KM=170 uM for ATP {ECO:0000269|PubMed:1445232};
CC       pH dependence:
CC         Optimum pH is between 8.5 and 9.0. {ECO:0000269|PubMed:1445232};
CC   -!- PATHWAY: Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis;
CC       pimeloyl-CoA from pimelate: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1445232}.
CC   -!- SIMILARITY: Belongs to the BioW family. {ECO:0000305}.
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; M29291; AAA22270.1; -; Genomic_DNA.
DR   PIR; JQ0511; JQ0511.
DR   RefSeq; WP_029747250.1; NZ_UFSZ01000001.1.
DR   AlphaFoldDB; P22822; -.
DR   SMR; P22822; -.
DR   GeneID; 48278543; -.
DR   BioCyc; MetaCyc:MON-14017; -.
DR   UniPathway; UPA00999; UER00351.
DR   GO; GO:0042410; F:6-carboxyhexanoate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009102; P:biotin biosynthetic process; IDA:UniProtKB.
DR   HAMAP; MF_00668; BioW; 1.
DR   InterPro; IPR005499; BioW.
DR   Pfam; PF03744; BioW; 1.
DR   TIGRFAMs; TIGR01204; bioW; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Biotin biosynthesis; Direct protein sequencing; Ligase;
KW   Magnesium; Nucleotide-binding.
FT   CHAIN           1..245
FT                   /note="6-carboxyhexanoate--CoA ligase"
FT                   /id="PRO_0000191015"
FT   CONFLICT        3..4
FT                   /note="ET -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  27591 MW;  B1407C8D70F570EC CRC64;
     MLETCYSIRM RAAEKNLEGG EKHISGGERI GSEFQIEPIV KQLLNKARNH SRGDADFIQI
     TVEKLTGDQI LYMPPLEITT IDESSIERAH KEARSILTSV GVSKQAQNVA FHLLASNQNL
     RGAILLHSQT GLRLDNRGLK GVRVSRIDWQ DADVGYNERV REALALATKV ANSPYTIAEL
     CWSDDPEYVT GYVSNHEIGY VRITPLKREG CESGGRIFFV SDEVELESYI HYLEREPILI
     RGHLK