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Database: UniProt
Entry: V2JH05_9BURK
LinkDB: V2JH05_9BURK
Original site: V2JH05_9BURK 
ID   V2JH05_9BURK            Unreviewed;       138 AA.
AC   V2JH05;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   13-SEP-2023, entry version 41.
DE   RecName: Full=Methylglyoxal synthase {ECO:0000256|HAMAP-Rule:MF_00549};
DE            Short=MGS {ECO:0000256|HAMAP-Rule:MF_00549};
DE            EC=4.2.3.3 {ECO:0000256|HAMAP-Rule:MF_00549};
GN   Name=mgsA {ECO:0000256|HAMAP-Rule:MF_00549};
GN   ORFNames=B551_0204950 {ECO:0000313|EMBL:ESJ24694.1};
OS   Cupriavidus sp. HPC(L).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ24694.1, ECO:0000313|Proteomes:UP000053474};
RN   [1] {ECO:0000313|EMBL:ESJ24694.1, ECO:0000313|Proteomes:UP000053474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA   Purohit H.J., Agarwal L.;
RT   "Cupriavidus a Desert isolate.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of methylglyoxal from
CC       dihydroxyacetone phosphate. {ECO:0000256|HAMAP-Rule:MF_00549}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate;
CC         Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00549};
CC   -!- SIMILARITY: Belongs to the methylglyoxal synthase family.
CC       {ECO:0000256|ARBA:ARBA00006287, ECO:0000256|HAMAP-Rule:MF_00549}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESJ24694.1}.
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DR   EMBL; AMPR02000056; ESJ24694.1; -; Genomic_DNA.
DR   RefSeq; WP_006579829.1; NZ_AMPR02000056.1.
DR   AlphaFoldDB; V2JH05; -.
DR   OrthoDB; 9787147at2; -.
DR   Proteomes; UP000053474; Unassembled WGS sequence.
DR   GO; GO:0008929; F:methylglyoxal synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019242; P:methylglyoxal biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01422; MGS; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00549; Methylglyoxal_synth; 1.
DR   InterPro; IPR004363; Methylgl_synth.
DR   InterPro; IPR018148; Methylglyoxal_synth_AS.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   NCBIfam; TIGR00160; MGSA; 1.
DR   PANTHER; PTHR30492; METHYLGLYOXAL SYNTHASE; 1.
DR   PANTHER; PTHR30492:SF0; METHYLGLYOXAL SYNTHASE; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF006614; Methylglyox_syn; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00549};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053474}.
FT   DOMAIN          4..138
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   ACT_SITE        70
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549,
FT                   ECO:0000256|PIRSR:PIRSR006614-1"
FT   BINDING         18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT   BINDING         44..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT   BINDING         64..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
SQ   SEQUENCE   138 AA;  14852 MW;  23C3D50ABC58623F CRC64;
     MTTTPVAAVP PRIALIAHDR KKDDIVAFAR RHRDFLVHCE LLATGTTGGR LIDEVGLSVT
     RMLSGPWGGD LQIGAQLAEG RVAAVIFLRD PMTPQPHEPD INALVRACDV HDVPCATNVA
     TADMLIAEMR RRAEAPAA
//
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