BIOW_THEYD
ID BIOW_THEYD Reviewed; 245 AA.
AC B5YK86;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, 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=THEYE_A0810;
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirae; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87;
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) 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; CP001147; ACI21089.1; -; Genomic_DNA.
DR RefSeq; YP_002248651.1; NC_011296.1.
DR AlphaFoldDB; B5YK86; -.
DR SMR; B5YK86; -.
DR STRING; 289376.THEYE_A0810; -.
DR EnsemblBacteria; ACI21089; ACI21089; THEYE_A0810.
DR KEGG; tye:THEYE_A0810; -.
DR PATRIC; fig|289376.4.peg.800; -.
DR eggNOG; COG1424; Bacteria.
DR HOGENOM; CLU_076858_0_0_0; -.
DR InParanoid; B5YK86; -.
DR OMA; LCWSDDP; -.
DR OrthoDB; 1268552at2; -.
DR UniPathway; UPA00999; UER00351.
DR Proteomes; UP000000718; 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_0000412092"
SQ SEQUENCE 245 AA; 27958 MW; A24D22D56921DE49 CRC64;
MWSVRMRASK KENNIEKHIS GAEGIYDYSQ IERVLKQLFK RAFEHSKGKP DKVVITVERI
NEEIQTVSAL PVNTFFTNSP EEAFCLISEK LSSIGISDKA LFSAFEVIKK YPMRGATLID
SITGERLERD KTRGIRVSRI HMDKRKRMKL IRQIKNLSTQ PQRVIEAITI ASKVASYPEV
VAELCISDNP DYTIGYIASR DLGYLRITNI KNKGETIGGR AFFVKTPCDI EKLTNYLERK
PVLVI
