ID A0A0F5ERG0_AVIPA Unreviewed; 149 AA.
AC A0A0F5ERG0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ECO:0000313|EMBL:SUU98584.1};
GN ORFNames=EIG79_00640 {ECO:0000313|EMBL:RZN61582.1}, HBL79_04460
GN {ECO:0000313|EMBL:QIR11558.1}, NCTC10926_02021
GN {ECO:0000313|EMBL:SUU98584.1}, NCTC11296_01323
GN {ECO:0000313|EMBL:STO71423.1};
OS Avibacterium paragallinarum (Haemophilus gallinarum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Avibacterium.
OX NCBI_TaxID=728 {ECO:0000313|EMBL:SUU98584.1, ECO:0000313|Proteomes:UP000254620};
RN [1] {ECO:0000313|Proteomes:UP000254465, ECO:0000313|Proteomes:UP000254620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10926 {ECO:0000313|EMBL:SUU98584.1,
RC ECO:0000313|Proteomes:UP000254620}, and NCTC11296
RC {ECO:0000313|EMBL:STO71423.1, ECO:0000313|Proteomes:UP000254465};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RZN61582.1, ECO:0000313|Proteomes:UP000294229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-3 {ECO:0000313|EMBL:RZN61582.1,
RC ECO:0000313|Proteomes:UP000294229};
RA Hellmuth J.E., Boucher C.E., Cason E.D.;
RT "Sequencing Av. paragallinarum serogroups.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QIR11558.1, ECO:0000313|Proteomes:UP000503595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESV-135 {ECO:0000313|EMBL:QIR11558.1,
RC ECO:0000313|Proteomes:UP000503595};
RA Cobos-Justo M.E., Sanchez-Alonso M.P., Negrete-Abascal E., Perez V.,
RA Soriano-Vargas E., Castelan H., Vazquez-Cruz C.;
RT "Comparison of the genome sequence of three Mexican strains of Avibacterium
RT paragallinarum.";
RL Submitted (MAR-2020) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP050316; QIR11558.1; -; Genomic_DNA.
DR EMBL; RQXS01000001; RZN61582.1; -; Genomic_DNA.
DR EMBL; UGHK01000002; STO71423.1; -; Genomic_DNA.
DR EMBL; UFSW01000001; SUU98584.1; -; Genomic_DNA.
DR RefSeq; WP_017807593.1; NZ_VXDA01000020.1.
DR STRING; 728.VY92_06695; -.
DR GeneID; 66255846; -.
DR KEGG; apag:EIA51_05310; -.
DR eggNOG; COG1803; Bacteria.
DR OrthoDB; 9787147at2; -.
DR Proteomes; UP000254465; Unassembled WGS sequence.
DR Proteomes; UP000254620; Unassembled WGS sequence.
DR Proteomes; UP000294229; Unassembled WGS sequence.
DR Proteomes; UP000503595; 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; 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, ECO:0000313|EMBL:SUU98584.1}.
FT DOMAIN 3..149
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 68
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549,
FT ECO:0000256|PIRSR:PIRSR006614-1"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 42..45
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 62..63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00549"
SQ SEQUENCE 149 AA; 16924 MW; FAD31C6D5087C5CE CRC64;
MIRQLSKHKN IALVAHDHCK EKLINWCKKH RALLEKHFLY ATGTTGNLIQ TEVNLTVNAL
LSGPMGGDQQ LGALIAEKKI DILIFFWDPM NAVPHDPDVK ALMRIATVWN IPVAMNVASA
DFIIYSELFH QETDICIPNY DGYLKERLK
//
