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Protein

L-glyceraldehyde 3-phosphate reductase

Gene

gpr

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). The physiological role of gpr is the detoxification of L-GAP, which may be formed by non-enzymatic racemization of GAP. Also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.3 Publications

Kineticsi

  1. KM=1.06 mM for 4-nitrobenzaldehyde (at pH 7 and at 25 degrees Celsius)1 Publication
  2. KM=3.4 mM for methylglyoxal (at pH 7 and at 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei61 – 611Important for catalysis
    Sitei66 – 661Important for catalysis
    Sitei97 – 971Important for catalysis
    Sitei138 – 1381Important for catalysis

    GO - Molecular functioni

    GO - Biological processi

    • cellular response to DNA damage stimulus Source: EcoliWiki
    • methylglyoxal metabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Enzyme and pathway databases

    BioCyciEcoCyc:G7558-MONOMER.
    ECOL316407:JW2970-MONOMER.
    MetaCyc:G7558-MONOMER.
    RETL1328306-WGS:GSTH-2473-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-glyceraldehyde 3-phosphate reductase (EC:1.1.1.-)
    Short name:
    GAP reductase
    Gene namesi
    Name:gpr
    Synonyms:mgrA, yghZ
    Ordered Locus Names:b3001, JW2970
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13010. gpr.

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show 23% decrease in the amount of acetol.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 346346L-glyceraldehyde 3-phosphate reductasePRO_0000201331Add
    BLAST

    Proteomic databases

    EPDiQ46851.
    PaxDbiQ46851.
    PRIDEiQ46851.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi4261416. 9 interactions.
    DIPiDIP-36026N.
    IntActiQ46851. 6 interactions.
    STRINGi511145.b3001.

    Structurei

    Secondary structure

    1
    346
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni7 – 104Combined sources
    Beta strandi15 – 173Combined sources
    Beta strandi24 – 318Combined sources
    Beta strandi33 – 353Combined sources
    Helixi42 – 5413Combined sources
    Beta strandi59 – 613Combined sources
    Turni67 – 715Combined sources
    Helixi72 – 8413Combined sources
    Turni86 – 883Combined sources
    Helixi89 – 913Combined sources
    Beta strandi93 – 986Combined sources
    Beta strandi103 – 1053Combined sources
    Beta strandi108 – 1114Combined sources
    Helixi113 – 12715Combined sources
    Beta strandi132 – 1376Combined sources
    Helixi146 – 15813Combined sources
    Beta strandi161 – 1699Combined sources
    Helixi172 – 18312Combined sources
    Turni184 – 1863Combined sources
    Beta strandi191 – 1933Combined sources
    Helixi202 – 2054Combined sources
    Helixi208 – 2158Combined sources
    Beta strandi218 – 2236Combined sources
    Helixi226 – 2316Combined sources
    Beta strandi240 – 2423Combined sources
    Turni243 – 2453Combined sources
    Helixi261 – 27616Combined sources
    Helixi281 – 2899Combined sources
    Beta strandi296 – 3005Combined sources
    Helixi305 – 3128Combined sources
    Helixi313 – 3164Combined sources
    Helixi322 – 33413Combined sources
    Helixi341 – 3444Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3N6QX-ray1.80A/B/C/D/E/F/G/H1-346[»]
    4ASTX-ray2.38A/B/C/D/E/F/G/H1-346[»]
    4AUBX-ray2.05A/B/C/D/E/F/G/H1-346[»]
    ProteinModelPortaliQ46851.
    SMRiQ46851. Positions 3-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CPC. Bacteria.
    COG0667. LUCA.
    HOGENOMiHOG000250283.
    InParanoidiQ46851.
    KOiK19265.
    OMAiTYIAAEN.
    OrthoDBiEOG6NSGJH.
    PhylomeDBiQ46851.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    SUPFAMiSSF51430. SSF51430. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q46851-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVWLANPERY GQMQYRYCGK SGLRLPALSL GLWHNFGHVN ALESQRAILR
    60 70 80 90 100
    KAFDLGITHF DLANNYGPPP GSAEENFGRL LREDFAAYRD ELIISTKAGY
    110 120 130 140 150
    DMWPGPYGSG GSRKYLLASL DQSLKRMGLE YVDIFYSHRV DENTPMEETA
    160 170 180 190 200
    SALAHAVQSG KALYVGISSY SPERTQKMVE LLREWKIPLL IHQPSYNLLN
    210 220 230 240 250
    RWVDKSGLLD TLQNNGVGCI AFTPLAQGLL TGKYLNGIPQ DSRMHREGNK
    260 270 280 290 300
    VRGLTPKMLT EANLNSLRLL NEMAQQRGQS MAQMALSWLL KDDRVTSVLI
    310 320 330 340
    GASRAEQLEE NVQALNNLTF STKELAQIDQ HIADGELNLW QASSDK
    Length:346
    Mass (Da):38,832
    Last modified:November 1, 1996 - v1
    Checksum:iC70D4D43A3A57AFC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28377 Genomic DNA. Translation: AAA69168.1.
    U00096 Genomic DNA. Translation: AAC76037.1.
    AP009048 Genomic DNA. Translation: BAE77060.1.
    PIRiG65086.
    RefSeqiNP_417474.1. NC_000913.3.
    WP_000262172.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76037; AAC76037; b3001.
    BAE77060; BAE77060; BAE77060.
    GeneIDi947480.
    KEGGiecj:JW2970.
    eco:b3001.
    PATRICi32121420. VBIEscCol129921_3097.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U28377 Genomic DNA. Translation: AAA69168.1.
    U00096 Genomic DNA. Translation: AAC76037.1.
    AP009048 Genomic DNA. Translation: BAE77060.1.
    PIRiG65086.
    RefSeqiNP_417474.1. NC_000913.3.
    WP_000262172.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3N6QX-ray1.80A/B/C/D/E/F/G/H1-346[»]
    4ASTX-ray2.38A/B/C/D/E/F/G/H1-346[»]
    4AUBX-ray2.05A/B/C/D/E/F/G/H1-346[»]
    ProteinModelPortaliQ46851.
    SMRiQ46851. Positions 3-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261416. 9 interactions.
    DIPiDIP-36026N.
    IntActiQ46851. 6 interactions.
    STRINGi511145.b3001.

    Proteomic databases

    EPDiQ46851.
    PaxDbiQ46851.
    PRIDEiQ46851.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76037; AAC76037; b3001.
    BAE77060; BAE77060; BAE77060.
    GeneIDi947480.
    KEGGiecj:JW2970.
    eco:b3001.
    PATRICi32121420. VBIEscCol129921_3097.

    Organism-specific databases

    EchoBASEiEB2831.
    EcoGeneiEG13010. gpr.

    Phylogenomic databases

    eggNOGiENOG4105CPC. Bacteria.
    COG0667. LUCA.
    HOGENOMiHOG000250283.
    InParanoidiQ46851.
    KOiK19265.
    OMAiTYIAAEN.
    OrthoDBiEOG6NSGJH.
    PhylomeDBiQ46851.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7558-MONOMER.
    ECOL316407:JW2970-MONOMER.
    MetaCyc:G7558-MONOMER.
    RETL1328306-WGS:GSTH-2473-MONOMER.

    Miscellaneous databases

    PROiQ46851.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red/Kv-b.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    SUPFAMiSSF51430. SSF51430. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. "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.
    3. "A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity."
      Grant A.W., Steel G., Waugh H., Ellis E.M.
      FEMS Microbiol. Lett. 218:93-99(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE METHYLGLYOXAL DETOXIFICATION AND AS A REDUCTASE.
    4. "Conversion of methylglyoxal to acetol by Escherichia coli aldo-keto reductases."
      Ko J., Kim I., Yoo S., Min B., Kim K., Park C.
      J. Bacteriol. 187:5782-5789(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE METHYLGLYOXAL DETOXIFICATION AND DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "A metabolic bypass of the triosephosphate isomerase reaction."
      Desai K.K., Miller B.G.
      Biochemistry 47:7983-7985(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A GLYCERALDEHYDE 3-PHOSPHATE REDUCTASE.
    6. "Macro-to-micro structural proteomics: native source proteins for high-throughput crystallization."
      Totir M., Echols N., Nanao M., Gee C.L., Moskaleva A., Gradia S., Iavarone A.T., Berger J.M., May A.P., Zubieta C., Alber T.
      PLoS ONE 7:E32498-E32498(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiGPR_ECOLI
    AccessioniPrimary (citable) accession number: Q46851
    Secondary accession number(s): Q2M9J6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: November 1, 1996
    Last modified: March 16, 2016
    This is version 111 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, 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.