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P0A731

- MGSA_ECOLI

UniProt

P0A731 - MGSA_ECOLI

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Protein

Methylglyoxal synthase

Gene

mgsA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Glycerone phosphate = methylglyoxal + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711

GO - Molecular functioni

  1. methylglyoxal synthase activity Source: EcoCyc

GO - Biological processi

  1. methylglyoxal biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciEcoCyc:METHGLYSYN-MONOMER.
ECOL316407:JW5129-MONOMER.
MetaCyc:METHGLYSYN-MONOMER.
BRENDAi4.2.3.3. 2026.
SABIO-RKP0A731.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylglyoxal synthase (EC:4.2.3.3)
Short name:
MGS
Gene namesi
Name:mgsA
Synonyms:yccG
Ordered Locus Names:b0963, JW5129
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG12307. mgsA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Methylglyoxal synthasePRO_0000178625Add
BLAST

Proteomic databases

PaxDbiP0A731.

Expressioni

Gene expression databases

GenevestigatoriP0A731.

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

BioGridi849948. 1 interaction.
DIPiDIP-48252N.
STRINGi511145.b0963.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Beta strandi13 – 186
Helixi20 – 223
Helixi23 – 3210
Helixi34 – 374
Beta strandi40 – 456
Helixi48 – 569
Beta strandi61 – 633
Helixi66 – 683
Helixi70 – 7910
Beta strandi85 – 895
Helixi99 – 11113
Beta strandi116 – 1194
Helixi120 – 1278
Helixi130 – 1334
Beta strandi136 – 1416
Helixi143 – 1475

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B93X-ray1.90A/B/C1-152[»]
1EGHX-ray2.00A/B/C/D/E/F1-152[»]
1IK4X-ray2.00A/B/C/D/E/F1-152[»]
1S89X-ray2.22A/B/C/D/E/F1-152[»]
1S8AX-ray2.20A/B/C/D/E/F1-152[»]
ProteinModelPortaliP0A731.
SMRiP0A731. Positions 1-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A731.

Family & Domainsi

Sequence similaritiesi

Belongs to the methylglyoxal synthase family.Curated

Phylogenomic databases

eggNOGiCOG1803.
HOGENOMiHOG000283729.
InParanoidiP0A731.
KOiK01734.
OMAiFFWDPFE.
OrthoDBiEOG644ZN1.
PhylomeDBiP0A731.

Family and domain databases

Gene3Di3.40.50.1380. 1 hit.
HAMAPiMF_00549. Methylglyoxal_synth.
InterProiIPR004363. Methylgl_synth.
IPR018148. Methylglyoxal_synth_AS.
IPR011607. MGS-like_dom.
[Graphical view]
PfamiPF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF006614. Methylglyox_syn. 1 hit.
SMARTiSM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
TIGRFAMsiTIGR00160. MGSA. 1 hit.
PROSITEiPS01335. METHYLGLYOXAL_SYNTH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A731-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELTTRTLPA RKHIALVAHD HCKQMLMSWV ERHQPLLEQH VLYATGTTGN
60 70 80 90 100
LISRATGMNV NAMLSGPMGG DQQVGALISE GKIDVLIFFW DPLNAVPHDP
110 120 130 140 150
DVKALLRLAT VWNIPVATNV ATADFIIQSP HFNDAVDILI PDYQRYLADR

LK
Length:152
Mass (Da):16,919
Last modified:June 7, 2005 - v1
Checksum:i85157193BD4CE72D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22ME → WK in J04726. (PubMed:2542273)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04726 Genomic DNA. No translation available.
Y11249 Genomic DNA. Translation: CAA72119.1.
U00096 Genomic DNA. Translation: AAC74049.2.
AP009048 Genomic DNA. Translation: BAA35728.2.
PIRiB64837.
RefSeqiNP_415483.2. NC_000913.3.
YP_489235.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74049; AAC74049; b0963.
BAA35728; BAA35728; BAA35728.
GeneIDi12931944.
945574.
KEGGiecj:Y75_p0935.
eco:b0963.
PATRICi32117145. VBIEscCol129921_0997.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04726 Genomic DNA. No translation available.
Y11249 Genomic DNA. Translation: CAA72119.1 .
U00096 Genomic DNA. Translation: AAC74049.2 .
AP009048 Genomic DNA. Translation: BAA35728.2 .
PIRi B64837.
RefSeqi NP_415483.2. NC_000913.3.
YP_489235.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B93 X-ray 1.90 A/B/C 1-152 [» ]
1EGH X-ray 2.00 A/B/C/D/E/F 1-152 [» ]
1IK4 X-ray 2.00 A/B/C/D/E/F 1-152 [» ]
1S89 X-ray 2.22 A/B/C/D/E/F 1-152 [» ]
1S8A X-ray 2.20 A/B/C/D/E/F 1-152 [» ]
ProteinModelPortali P0A731.
SMRi P0A731. Positions 1-151.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 849948. 1 interaction.
DIPi DIP-48252N.
STRINGi 511145.b0963.

Proteomic databases

PaxDbi P0A731.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74049 ; AAC74049 ; b0963 .
BAA35728 ; BAA35728 ; BAA35728 .
GeneIDi 12931944.
945574.
KEGGi ecj:Y75_p0935.
eco:b0963.
PATRICi 32117145. VBIEscCol129921_0997.

Organism-specific databases

EchoBASEi EB2213.
EcoGenei EG12307. mgsA.

Phylogenomic databases

eggNOGi COG1803.
HOGENOMi HOG000283729.
InParanoidi P0A731.
KOi K01734.
OMAi FFWDPFE.
OrthoDBi EOG644ZN1.
PhylomeDBi P0A731.

Enzyme and pathway databases

BioCyci EcoCyc:METHGLYSYN-MONOMER.
ECOL316407:JW5129-MONOMER.
MetaCyc:METHGLYSYN-MONOMER.
BRENDAi 4.2.3.3. 2026.
SABIO-RK P0A731.

Miscellaneous databases

EvolutionaryTracei P0A731.
PROi P0A731.

Gene expression databases

Genevestigatori P0A731.

Family and domain databases

Gene3Di 3.40.50.1380. 1 hit.
HAMAPi MF_00549. Methylglyoxal_synth.
InterProi IPR004363. Methylgl_synth.
IPR018148. Methylglyoxal_synth_AS.
IPR011607. MGS-like_dom.
[Graphical view ]
Pfami PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF006614. Methylglyox_syn. 1 hit.
SMARTi SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
TIGRFAMsi TIGR00160. MGSA. 1 hit.
PROSITEi PS01335. METHYLGLYOXAL_SYNTH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The molecular cloning of the gene encoding the Escherichia coli 75-kDa helicase and the determination of its nucleotide sequence and gentic map position."
    Wood E.R., Matson S.W.
    J. Biol. Chem. 264:8297-8303(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "From famine to feast: the role of methylglyoxal production in Escherichia coli."
    Totemeyer S., Booth N.A., Nichols W.W., Dunbar B., Booth I.R.
    Mol. Microbiol. 27:553-562(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
    Borodovsky M., Rudd K.E., Koonin E.V.
    Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "Identification of catalytic bases in the active site of Escherichia coli methylglyoxal synthase: cloning, expression, and functional characterization of conserved aspartic acid residues."
    Saadat D., Harrison D.H.T.
    Biochemistry 37:10074-10086(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASPARTIC ACID RESIDUES.
  8. "The crystal structure of methylglyoxal synthase from Escherichia coli."
    Saadat D., Harrison D.H.T.
    Structure 7:309-317(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  9. "Mirroring perfection: the structure of methylglyoxal synthase complexed with the competitive inhibitor 2-phosphoglycolate."
    Saadat D., Harrison D.H.T.
    Biochemistry 39:2950-2960(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiMGSA_ECOLI
AccessioniPrimary (citable) accession number: P0A731
Secondary accession number(s): P37066
, P75872, Q8XD91, Q9R7Q3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: October 29, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3