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Database: UniProt
Entry: W7YWR5_9BACL
LinkDB: W7YWR5_9BACL
Original site: W7YWR5_9BACL 
ID   W7YWR5_9BACL            Unreviewed;       140 AA.
AC   W7YWR5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=JCM16418_3209 {ECO:0000313|EMBL:GAF09091.1};
OS   Paenibacillus pini JCM 16418.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF09091.1, ECO:0000313|Proteomes:UP000019364};
RN   [1] {ECO:0000313|EMBL:GAF09091.1, ECO:0000313|Proteomes:UP000019364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF09091.1,
RC   ECO:0000313|Proteomes:UP000019364};
RA   Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from the
RT   Rhizosphere of Pine Tree.";
RL   Genome Announc. 2:e00210-14(2014).
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|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:GAF09091.1}.
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DR   EMBL; BAVZ01000009; GAF09091.1; -; Genomic_DNA.
DR   RefSeq; WP_036650155.1; NZ_BAZT01000009.1.
DR   AlphaFoldDB; W7YWR5; -.
DR   STRING; 1236976.JCM16418_3209; -.
DR   eggNOG; COG1803; Bacteria.
DR   OrthoDB; 9787147at2; -.
DR   Proteomes; UP000019364; 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:UP000019364}.
FT   DOMAIN          1..140
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   ACT_SITE        61
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549,
FT                   ECO:0000256|PIRSR:PIRSR006614-1"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT   BINDING         35..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT   BINDING         55..56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
SQ   SEQUENCE   140 AA;  15754 MW;  DBA523F582A5F28F CRC64;
     MLKIAFIAHD RKKDEMVNFV TAYEHVFEGH KLYSTGTTGQ RIMEGTALRI HRFMSGPLGG
     DQQIGALVAQ NEMDLIIFLR DPLMAQPHEP DINALLRLCD VQGIPLATNI ATAEILVKAL
     ERGDFAWREL VHKYKPGEEV
//
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