MGSA_COXBN
ID MGSA_COXBN Reviewed; 143 AA.
AC A9KFK7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Methylglyoxal synthase {ECO:0000255|HAMAP-Rule:MF_00549};
DE Short=MGS {ECO:0000255|HAMAP-Rule:MF_00549};
DE EC=4.2.3.3 {ECO:0000255|HAMAP-Rule:MF_00549};
GN Name=mgsA {ECO:0000255|HAMAP-Rule:MF_00549}; OrderedLocusNames=CBUD_0918;
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
CC -!- FUNCTION: Catalyzes the formation of methylglyoxal from
CC dihydroxyacetone phosphate. {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00549};
CC -!- SIMILARITY: Belongs to the methylglyoxal synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00549}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS78087.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000733; ABS78087.2; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A9KFK7; -.
DR SMR; A9KFK7; -.
DR EnsemblBacteria; ABS78087; ABS78087; CBUD_0918.
DR KEGG; cbd:CBUD_0918; -.
DR HOGENOM; CLU_120420_0_1_6; -.
DR OMA; RACDVHN; -.
DR Proteomes; UP000008555; Chromosome.
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; -; 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 PANTHER; PTHR30492; PTHR30492; 1.
DR Pfam; PF02142; MGS; 1.
DR PIRSF; PIRSF006614; Methylglyox_syn; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR TIGRFAMs; TIGR00160; MGSA; 1.
DR PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Lyase.
FT CHAIN 1..143
FT /note="Methylglyoxal synthase"
FT /id="PRO_1000081953"
FT DOMAIN 1..143
FT /note="MGS-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT ACT_SITE 63
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 37..40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 57..58
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
SQ SEQUENCE 143 AA; 16233 MW; 30F7FCD5052B10CD CRC64;
MTVKKIALVA HDRMKKELIE WIKKHQNLLK HHELYATGST GQAIEKTLNV TVTKMESGPL
GGDLQLGAKI VNKEIDILIF FWDPLEAQPH DPDVRALLRI AVVWNLPVAC NASTADYLLT
SPLFDSDYHP ETPDYEAYRN RII
