BIOW_METVM
ID BIOW_METVM Reviewed; 233 AA.
AC C9REY1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 49.
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=Metvu_0266;
OS Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
OS (Methanococcus vulcanius).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=579137;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700851 / DSM 12094 / M7;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lcollab F.I., Brettin T., Detter J.C.,
RA Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinikova G., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus vulcanius M7.";
RL Submitted (OCT-2009) 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; CP001787; ACX72133.1; -; Genomic_DNA.
DR RefSeq; WP_012819677.1; NC_013407.1.
DR AlphaFoldDB; C9REY1; -.
DR SMR; C9REY1; -.
DR STRING; 579137.Metvu_0266; -.
DR EnsemblBacteria; ACX72133; ACX72133; Metvu_0266.
DR GeneID; 8512595; -.
DR KEGG; mvu:Metvu_0266; -.
DR eggNOG; arCOG05075; Archaea.
DR HOGENOM; CLU_076858_0_0_2; -.
DR OMA; LCWSDDP; -.
DR OrthoDB; 68002at2157; -.
DR UniPathway; UPA00999; UER00351.
DR Proteomes; UP000002063; 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.
FT CHAIN 1..233
FT /note="6-carboxyhexanoate--CoA ligase"
FT /id="PRO_0000412097"
SQ SEQUENCE 233 AA; 26314 MW; E027E402ED275CD1 CRC64;
MYSIKMRASK NGKHISGAER IVEKEKIEEV VKDLTKRALN HENGTPDFIN IKVEKIVGEI
EYIDHLPIIT IPCKNIKEAR KKAIEILINE GIPKEIILQA FEIIDRGGMR GAALLNLKGE
RLDPDKERGV RVKNIDVSES LKNEILTKNL GTERTVDAIA IASKVIHLGV LAELCTSDNK
NYTTGYVATK KGYFRITNLK REGDPGGRVF FIKDDRNIKK LIEKLENKPC IIR