BIOW_METMP
ID BIOW_METMP Reviewed; 244 AA.
AC Q6LWX9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=MMP1575;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF31131.1; -; Genomic_DNA.
DR RefSeq; WP_011171519.1; NC_005791.1.
DR AlphaFoldDB; Q6LWX9; -.
DR SMR; Q6LWX9; -.
DR STRING; 267377.MMP1575; -.
DR EnsemblBacteria; CAF31131; CAF31131; MMP1575.
DR GeneID; 2761285; -.
DR KEGG; mmp:MMP1575; -.
DR PATRIC; fig|267377.15.peg.1613; -.
DR eggNOG; arCOG05075; Archaea.
DR HOGENOM; CLU_076858_0_0_2; -.
DR OMA; LCWSDDP; -.
DR OrthoDB; 68002at2157; -.
DR BioCyc; MMAR267377:MMP_RS08105-MON; -.
DR UniPathway; UPA00999; UER00351.
DR Proteomes; UP000000590; 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.
PE 3: Inferred from homology;
KW ATP-binding; Biotin biosynthesis; Ligase; Magnesium; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..244
FT /note="6-carboxyhexanoate--CoA ligase"
FT /id="PRO_0000412102"
SQ SEQUENCE 244 AA; 27453 MW; 0DD8F18940102B69 CRC64;
MFSLKMRASS NGNHVSGAER LVKEEQIEEI SSELIKRAMN HENGVPDFIN LKVEKVTENI
NYIEHLKIKT INSNSKETSR EFAINILKKE LENYFLKNGK DTKKIDELID SAFKIIDAGN
MRGAAILDLD GNRLEKSSDR GIRVRNIDTA EELSKKILKD GSLTERTVDA IAIATKVVNC
DIIAELCTSD NFSYTTGYVA TKDGYFRILN LKDSGQVGGR VFFAESSDID ELYDKLENMP
VIVY