Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A731

- MGSA_ECOLI

UniProt

P0A731 - MGSA_ECOLI

Protein

Methylglyoxal synthase

Gene

mgsA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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-SubCell

    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.
    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

    MELTTRTLPA RKHIALVAHD HCKQMLMSWV ERHQPLLEQH VLYATGTTGN    50
    LISRATGMNV NAMLSGPMGG DQQVGALISE GKIDVLIFFW DPLNAVPHDP 100
    DVKALLRLAT VWNIPVATNV ATADFIIQSP HFNDAVDILI PDYQRYLADR 150
    LK 152
    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.
    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

    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 1, 2014
    This is version 79 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