Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A731 (MGSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylglyoxal synthase

Short name=MGS
EC=4.2.3.3
Gene names
Name:mgsA
Synonyms:yccG
Ordered Locus Names:b0963, JW5129
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Glycerone phosphate = methylglyoxal + phosphate. HAMAP-Rule MF_00549

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00549.

Sequence similarities

Belongs to the methylglyoxal synthase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmethylglyoxal biosynthetic process

Inferred from mutant phenotype PubMed 15489434. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmethylglyoxal synthase activity

Inferred from direct assay PubMed 4563643. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Methylglyoxal synthase HAMAP-Rule MF_00549
PRO_0000178625

Sites

Active site711

Experimental info

Sequence conflict1 – 22ME → WK in J04726. Ref.1

Secondary structure

................................. 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A731 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 85157193BD4CE72D

FASTA15216,919
        10         20         30         40         50         60 
MELTTRTLPA RKHIALVAHD HCKQMLMSWV ERHQPLLEQH VLYATGTTGN LISRATGMNV 

        70         80         90        100        110        120 
NAMLSGPMGG DQQVGALISE GKIDVLIFFW DPLNAVPHDP DVKALLRLAT VWNIPVATNV 

       130        140        150 
ATADFIIQSP HFNDAVDILI PDYQRYLADR LK 

« Hide

References

« Hide 'large scale' references
[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]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04726 Genomic DNA. No translation available.
Y11249 Genomic DNA. Translation: CAA72119.1.
U00096 Genomic DNA. Translation: AAC74049.2.
AP009048 Genomic DNA. Translation: BAA35728.2.
PIRB64837.
RefSeqNP_415483.2. NC_000913.3.
YP_489235.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0A731.
SMRP0A731. Positions 1-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid849948. 1 interaction.
DIPDIP-48252N.
STRING511145.b0963.

Proteomic databases

PaxDbP0A731.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74049; AAC74049; b0963.
BAA35728; BAA35728; BAA35728.
GeneID12931944.
945574.
KEGGecj:Y75_p0935.
eco:b0963.
PATRIC32117145. VBIEscCol129921_0997.

Organism-specific databases

EchoBASEEB2213.
EcoGeneEG12307. mgsA.

Phylogenomic databases

eggNOGCOG1803.
HOGENOMHOG000283729.
KOK01734.
OMAFFWDPFE.
OrthoDBEOG644ZN1.
PhylomeDBP0A731.

Enzyme and pathway databases

BioCycEcoCyc:METHGLYSYN-MONOMER.
ECOL316407:JW5129-MONOMER.
MetaCyc:METHGLYSYN-MONOMER.
BRENDA4.2.3.3. 2026.
SABIO-RKP0A731.

Gene expression databases

GenevestigatorP0A731.

Family and domain databases

Gene3D3.40.50.1380. 1 hit.
HAMAPMF_00549. Methylglyoxal_synth.
InterProIPR004363. Methylgl_synth.
IPR018148. Methylglyoxal_synth_AS.
IPR011607. MGS-like_dom.
[Graphical view]
PfamPF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF006614. Methylglyox_syn. 1 hit.
SMARTSM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
TIGRFAMsTIGR00160. MGSA. 1 hit.
PROSITEPS01335. METHYLGLYOXAL_SYNTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A731.
PROP0A731.

Entry information

Entry nameMGSA_ECOLI
AccessionPrimary (citable) accession number: P0A731
Secondary accession number(s): P37066 expand/collapse secondary AC list , P75872, Q8XD91, Q9R7Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: May 14, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene