MGSA_BACSU
ID MGSA_BACSU Reviewed; 137 AA.
AC P42980;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
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}; Synonyms=ypjF;
GN OrderedLocusNames=BSU22480;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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, ECO:0000305}.
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DR EMBL; L38424; AAA92875.1; -; Genomic_DNA.
DR EMBL; L47709; AAB38443.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14164.1; -; Genomic_DNA.
DR PIR; E69937; E69937.
DR RefSeq; NP_390129.1; NC_000964.3.
DR RefSeq; WP_003230640.1; NZ_JNCM01000036.1.
DR PDB; 6F2C; X-ray; 2.34 A; A/B/C/D/E/F/G/H/I/J/K/L=1-137.
DR PDBsum; 6F2C; -.
DR AlphaFoldDB; P42980; -.
DR SMR; P42980; -.
DR STRING; 224308.BSU22480; -.
DR PaxDb; P42980; -.
DR PRIDE; P42980; -.
DR EnsemblBacteria; CAB14164; CAB14164; BSU_22480.
DR GeneID; 939027; -.
DR KEGG; bsu:BSU22480; -.
DR PATRIC; fig|224308.179.peg.2452; -.
DR eggNOG; COG1803; Bacteria.
DR InParanoid; P42980; -.
DR OMA; RACDVHN; -.
DR PhylomeDB; P42980; -.
DR BioCyc; BSUB:BSU22480-MON; -.
DR BRENDA; 4.2.3.3; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008929; F:methylglyoxal synthase activity; IDA:CACAO.
DR GO; GO:0019242; P:methylglyoxal biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome.
FT CHAIN 1..137
FT /note="Methylglyoxal synthase"
FT /id="PRO_0000178613"
FT DOMAIN 1..137
FT /note="MGS-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT ACT_SITE 60
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 34..37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 54..55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00549"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6F2C"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:6F2C"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:6F2C"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:6F2C"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6F2C"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:6F2C"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6F2C"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:6F2C"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:6F2C"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6F2C"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:6F2C"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:6F2C"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:6F2C"
SQ SEQUENCE 137 AA; 15128 MW; 01FC7883A3837F98 CRC64;
MKIALIAHDK KKQDMVQFTT AYRDILKNHD LYATGTTGLK IHEATGLQIE RFQSGPLGGD
QQIGALIAAN ALDLVIFLRD PLTAQPHEPD VSALIRLCDV YSIPLATNMG TAEILVRTLD
EGVFEFRDLL RGEEPNV
