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Protein

Glyceraldehyde-3-phosphate dehydrogenase A

Gene

gapA

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

Functioni

Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.1 Publication

Catalytic activityi

D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.1 Publication

Kineticsi

Kcat is 1056 sec(-1) for dehydrogenase activity.

  1. KM=15 µM for BPG1 Publication
  2. KM=42 µM for NAD1 Publication
  3. KM=1500 µM for G3P1 Publication

    Pathwayi: glycolysis

    This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.Curated
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Putative glyceraldehyde-3-phosphate dehydrogenase C (gapC), Glyceraldehyde-3-phosphate dehydrogenase A (gapA)
    2. Phosphoglycerate kinase (pgk)
    3. Probable phosphoglycerate mutase GpmB (gpmB), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
    4. Enolase (eno)
    5. Pyruvate kinase I (pykF), Pyruvate kinase II (pykA)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei34 – 341NAD3 Publications
    Binding sitei78 – 781NAD; via carbonyl oxygen2 Publications
    Binding sitei120 – 1201NAD1 Publication
    Active sitei150 – 1501Nucleophile1 Publication
    Sitei177 – 1771Activates thiol group during catalysis1 Publication
    Binding sitei180 – 1801Glyceraldehyde 3-phosphateBy similarity
    Binding sitei232 – 2321Glyceraldehyde 3-phosphate1 Publication2 Publications
    Binding sitei314 – 3141NAD3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 132NAD4 Publications

    GO - Molecular functioni

    • glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
    • NAD binding Source: UniProtKB
    • NADP binding Source: InterPro

    GO - Biological processi

    • glucose metabolic process Source: InterPro
    • glycolytic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    NAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:GAPDH-A-MONOMER.
    ECOL316407:JW1768-MONOMER.
    MetaCyc:GAPDH-A-MONOMER.
    BRENDAi1.2.1.12. 2026.
    SABIO-RKP0A9B2.
    UniPathwayiUPA00109; UER00184.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase A1 Publication (EC:1.2.1.121 Publication)
    Short name:
    GAPDH-A1 Publication
    Alternative name(s):
    NAD-dependent glyceraldehyde-3-phosphate dehydrogenase1 Publication
    Gene namesi
    Name:gapA1 Publication
    Ordered Locus Names:b1779, JW1768
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10367. gapA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi177 – 1771H → N: Reduces activity about 50-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved2 Publications
    Chaini2 – 331330Glyceraldehyde-3-phosphate dehydrogenase APRO_0000145648Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 1151N6-succinyllysine1 Publication
    Modified residuei124 – 1241N6-succinyllysine1 Publication
    Modified residuei132 – 1321N6-acetyllysine; alternate1 Publication
    Modified residuei132 – 1321N6-succinyllysine; alternate1 Publication
    Modified residuei138 – 1381N6-acetyllysine1 Publication
    Modified residuei192 – 1921N6-acetyllysine; alternate1 Publication
    Modified residuei192 – 1921N6-succinyllysine; alternate1 Publication
    Modified residuei213 – 2131N6-succinyllysine1 Publication
    Modified residuei217 – 2171N6-succinyllysine1 Publication
    Modified residuei225 – 2251N6-succinyllysine1 Publication
    Modified residuei249 – 2491N6-acetyllysine1 Publication
    Modified residuei249 – 2491N6-succinyllysine1 Publication
    Modified residuei257 – 2571N6-succinyllysine1 Publication
    Modified residuei261 – 2611N6-succinyllysine1 Publication
    Modified residuei331 – 3311N6-malonyllysine; alternate1 Publication
    Modified residuei331 – 3311N6-succinyllysine; alternate1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiP0A9B2.
    PaxDbiP0A9B2.
    PRIDEiP0A9B2.

    2D gel databases

    SWISS-2DPAGEP0A9B2.

    Interactioni

    Subunit structurei

    Homotetramer.3 Publications

    Protein-protein interaction databases

    BioGridi4260308. 24 interactions.
    851992. 1 interaction.
    DIPiDIP-31848N.
    IntActiP0A9B2. 25 interactions.
    MINTiMINT-1255410.
    STRINGi511145.b1779.

    Structurei

    Secondary structure

    1
    331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86Combined sources
    Helixi12 – 2211Combined sources
    Beta strandi25 – 339Combined sources
    Helixi38 – 469Combined sources
    Turni49 – 513Combined sources
    Beta strandi58 – 614Combined sources
    Beta strandi64 – 674Combined sources
    Beta strandi70 – 756Combined sources
    Helixi80 – 834Combined sources
    Helixi85 – 884Combined sources
    Beta strandi91 – 955Combined sources
    Beta strandi97 – 993Combined sources
    Helixi103 – 1064Combined sources
    Helixi108 – 1114Combined sources
    Beta strandi115 – 1217Combined sources
    Beta strandi124 – 1263Combined sources
    Turni132 – 1343Combined sources
    Helixi136 – 1383Combined sources
    Beta strandi143 – 1464Combined sources
    Helixi150 – 16617Combined sources
    Beta strandi168 – 17710Combined sources
    Beta strandi183 – 1875Combined sources
    Helixi194 – 1974Combined sources
    Turni200 – 2023Combined sources
    Beta strandi205 – 2084Combined sources
    Turni211 – 2144Combined sources
    Helixi215 – 2184Combined sources
    Helixi220 – 2223Combined sources
    Beta strandi225 – 2328Combined sources
    Beta strandi239 – 24911Combined sources
    Helixi253 – 26513Combined sources
    Turni266 – 2716Combined sources
    Beta strandi272 – 2754Combined sources
    Helixi281 – 2844Combined sources
    Beta strandi289 – 2946Combined sources
    Turni295 – 2973Combined sources
    Beta strandi299 – 3024Combined sources
    Beta strandi305 – 3128Combined sources
    Helixi316 – 32813Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DC3X-ray2.50A/B2-331[»]
    1DC4X-ray2.50A/B2-331[»]
    1DC5X-ray2.00A/B2-331[»]
    1DC6X-ray2.00A/B2-331[»]
    1GADX-ray1.80O/P2-331[»]
    1GAEX-ray2.17O/P2-331[»]
    1S7CX-ray2.04A1-331[»]
    2VYNX-ray2.20A/B/C1-331[»]
    2VYVX-ray2.38A/B/C1-331[»]
    ProteinModelPortaliP0A9B2.
    SMRiP0A9B2. Positions 2-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9B2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni149 – 1513Glyceraldehyde 3-phosphate binding1 Publication
    Regioni209 – 2102Glyceraldehyde 3-phosphate binding1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C17. Bacteria.
    COG0057. LUCA.
    HOGENOMiHOG000071678.
    InParanoidiP0A9B2.
    KOiK00134.
    OMAiKWGEVGA.
    OrthoDBiEOG66TG3S.
    PhylomeDBiP0A9B2.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10836. PTHR10836. 1 hit.
    PfamiPF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000149. GAP_DH. 1 hit.
    PRINTSiPR00078. G3PDHDRGNASE.
    SMARTiSM00846. Gp_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
    PROSITEiPS00071. GAPDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A9B2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTIKVGINGF GRIGRIVFRA AQKRSDIEIV AINDLLDADY MAYMLKYDST
    60 70 80 90 100
    HGRFDGTVEV KDGHLIVNGK KIRVTAERDP ANLKWDEVGV DVVAEATGLF
    110 120 130 140 150
    LTDETARKHI TAGAKKVVMT GPSKDNTPMF VKGANFDKYA GQDIVSNASC
    160 170 180 190 200
    TTNCLAPLAK VINDNFGIIE GLMTTVHATT ATQKTVDGPS HKDWRGGRGA
    210 220 230 240 250
    SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV VDLTVRLEKA
    260 270 280 290 300
    ATYEQIKAAV KAAAEGEMKG VLGYTEDDVV STDFNGEVCT SVFDAKAGIA
    310 320 330
    LNDNFVKLVS WYDNETGYSN KVLDLIAHIS K
    Length:331
    Mass (Da):35,532
    Last modified:January 23, 2007 - v2
    Checksum:iB3A460AA6D59E46D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431Y → I in strain: ECOR 70.
    Natural varianti266 – 2661G → D in strain: E830587.
    Natural varianti267 – 2671E → A in strain: E2666-74.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X02662 Genomic DNA. Translation: CAA26498.1.
    U00096 Genomic DNA. Translation: AAC74849.1.
    AP009048 Genomic DNA. Translation: BAA15576.1.
    M66870 Genomic DNA. Translation: AAA23838.1.
    M66871 Genomic DNA. Translation: AAA23839.1.
    M66872 Genomic DNA. Translation: AAA02930.1.
    M66873 Genomic DNA. Translation: AAA23840.1.
    M66874 Genomic DNA. Translation: AAA23841.1.
    M66875 Genomic DNA. Translation: AAA23842.1.
    M66876 Genomic DNA. Translation: AAA23843.1.
    M66877 Genomic DNA. Translation: AAA23844.1.
    M66878 Genomic DNA. Translation: AAA23845.1.
    M66879 Genomic DNA. Translation: AAA23846.1.
    M66880 Genomic DNA. Translation: AAA23847.1.
    M66881 Genomic DNA. Translation: AAA23848.1.
    M66882 Genomic DNA. Translation: AAA23849.1.
    U07750 Genomic DNA. Translation: AAC43271.1.
    U07751 Genomic DNA. Translation: AAC43272.1.
    U07752 Genomic DNA. Translation: AAC43273.1.
    U07754 Genomic DNA. Translation: AAC43274.1.
    U07765 Genomic DNA. Translation: AAC43284.1.
    U07768 Genomic DNA. Translation: AAC43285.1.
    U07769 Genomic DNA. Translation: AAC43286.1.
    U07770 Genomic DNA. Translation: AAC43287.1.
    U07771 Genomic DNA. Translation: AAC43288.1.
    U07772 Genomic DNA. Translation: AAC43289.1.
    U07773 Genomic DNA. Translation: AAC43290.1.
    PIRiA25209. DEECG3.
    RefSeqiNP_416293.1. NC_000913.3.
    WP_000153502.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74849; AAC74849; b1779.
    BAA15576; BAA15576; BAA15576.
    GeneIDi947679.
    KEGGiecj:JW1768.
    eco:b1779.
    PATRICi32118869. VBIEscCol129921_1852.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X02662 Genomic DNA. Translation: CAA26498.1.
    U00096 Genomic DNA. Translation: AAC74849.1.
    AP009048 Genomic DNA. Translation: BAA15576.1.
    M66870 Genomic DNA. Translation: AAA23838.1.
    M66871 Genomic DNA. Translation: AAA23839.1.
    M66872 Genomic DNA. Translation: AAA02930.1.
    M66873 Genomic DNA. Translation: AAA23840.1.
    M66874 Genomic DNA. Translation: AAA23841.1.
    M66875 Genomic DNA. Translation: AAA23842.1.
    M66876 Genomic DNA. Translation: AAA23843.1.
    M66877 Genomic DNA. Translation: AAA23844.1.
    M66878 Genomic DNA. Translation: AAA23845.1.
    M66879 Genomic DNA. Translation: AAA23846.1.
    M66880 Genomic DNA. Translation: AAA23847.1.
    M66881 Genomic DNA. Translation: AAA23848.1.
    M66882 Genomic DNA. Translation: AAA23849.1.
    U07750 Genomic DNA. Translation: AAC43271.1.
    U07751 Genomic DNA. Translation: AAC43272.1.
    U07752 Genomic DNA. Translation: AAC43273.1.
    U07754 Genomic DNA. Translation: AAC43274.1.
    U07765 Genomic DNA. Translation: AAC43284.1.
    U07768 Genomic DNA. Translation: AAC43285.1.
    U07769 Genomic DNA. Translation: AAC43286.1.
    U07770 Genomic DNA. Translation: AAC43287.1.
    U07771 Genomic DNA. Translation: AAC43288.1.
    U07772 Genomic DNA. Translation: AAC43289.1.
    U07773 Genomic DNA. Translation: AAC43290.1.
    PIRiA25209. DEECG3.
    RefSeqiNP_416293.1. NC_000913.3.
    WP_000153502.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DC3X-ray2.50A/B2-331[»]
    1DC4X-ray2.50A/B2-331[»]
    1DC5X-ray2.00A/B2-331[»]
    1DC6X-ray2.00A/B2-331[»]
    1GADX-ray1.80O/P2-331[»]
    1GAEX-ray2.17O/P2-331[»]
    1S7CX-ray2.04A1-331[»]
    2VYNX-ray2.20A/B/C1-331[»]
    2VYVX-ray2.38A/B/C1-331[»]
    ProteinModelPortaliP0A9B2.
    SMRiP0A9B2. Positions 2-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260308. 24 interactions.
    851992. 1 interaction.
    DIPiDIP-31848N.
    IntActiP0A9B2. 25 interactions.
    MINTiMINT-1255410.
    STRINGi511145.b1779.

    2D gel databases

    SWISS-2DPAGEP0A9B2.

    Proteomic databases

    EPDiP0A9B2.
    PaxDbiP0A9B2.
    PRIDEiP0A9B2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74849; AAC74849; b1779.
    BAA15576; BAA15576; BAA15576.
    GeneIDi947679.
    KEGGiecj:JW1768.
    eco:b1779.
    PATRICi32118869. VBIEscCol129921_1852.

    Organism-specific databases

    EchoBASEiEB0362.
    EcoGeneiEG10367. gapA.

    Phylogenomic databases

    eggNOGiENOG4105C17. Bacteria.
    COG0057. LUCA.
    HOGENOMiHOG000071678.
    InParanoidiP0A9B2.
    KOiK00134.
    OMAiKWGEVGA.
    OrthoDBiEOG66TG3S.
    PhylomeDBiP0A9B2.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00184.
    BioCyciEcoCyc:GAPDH-A-MONOMER.
    ECOL316407:JW1768-MONOMER.
    MetaCyc:GAPDH-A-MONOMER.
    BRENDAi1.2.1.12. 2026.
    SABIO-RKP0A9B2.

    Miscellaneous databases

    EvolutionaryTraceiP0A9B2.
    PROiP0A9B2.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10836. PTHR10836. 1 hit.
    PfamiPF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000149. GAP_DH. 1 hit.
    PRINTSiPR00078. G3PDHDRGNASE.
    SMARTiSM00846. Gp_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
    PROSITEiPS00071. GAPDH. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase."
      Branlant G., Branlant C.
      Eur. J. Biochem. 150:61-66(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Nelson K.
      Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 295-300.
    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. Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    8. "Nucleotide polymorphism and evolution in the glyceraldehyde-3-phosphate dehydrogenase gene (gapA) in natural populations of Salmonella and Escherichia coli."
      Nelson K., Whittam T.S., Selander R.K.
      Proc. Natl. Acad. Sci. U.S.A. 88:6667-6671(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-314.
      Strain: A8190, E2666-74, E3406, E830587, E851819, ECOR 14, ECOR 32, ECOR 40, ECOR 52, ECOR 58, ECOR 64 and ECOR 70.
    9. "Detecting selective sweeps in naturally occurring Escherichia coli."
      Guttman D.S., Dykhuizen D.E.
      Genetics 138:993-1003(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-321.
      Strain: ECOR 10, ECOR 16, ECOR 38, ECOR 39, ECOR 4, ECOR 40, ECOR 49, ECOR 65, ECOR 68, ECOR 8 and O2:HN / ECOR 50 / P97 / UPEC.
    10. "A naturally occurring horizontal gene transfer from a eukaryote to a prokaryote."
      Doolittle R.F., Feng D.F., Anderson K.L., Alberro M.R.
      J. Mol. Evol. 31:383-388(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE TRANSFER DISCUSSION.
    11. "Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis."
      Soukri A., Mougin A., Corbier C., Wonacott A., Branlant C., Branlant G.
      Biochemistry 28:2586-2592(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-177.
    12. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    13. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-138; LYS-192 AND LYS-249, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    14. Cited for: MALONYLATION AT LYS-331.
      Strain: K12.
    15. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-115; LYS-124; LYS-132; LYS-192; LYS-213; LYS-217; LYS-225; LYS-249; LYS-257; LYS-261 AND LYS-331.
      Strain: K12.
    16. "Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity."
      Duee E., Olivier-Deyris L., Fanchon E., Corbier C., Branlant G., Dideberg O.
      J. Mol. Biol. 257:814-838(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND THR-313 MUTANT IN COMPLEX WITH NAD, SUBUNIT.
    17. "Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli: direct evidence of substrate binding and cofactor-induced conformational changes."
      Yun M., Park C.-G., Kim J.-Y., Park H.-W.
      Biochemistry 39:10702-10710(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND GLYCERALDEHYDE 3-PHOSPHATE, SUBUNIT.
    18. "Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli."
      Shin D.H., Thor J., Yokota H., Kim R., Kim S.H.
      Submitted (JAN-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
    19. "Structure of insoluble rat sperm glyceraldehyde-3-phosphate dehydrogenase (GAPDH) via heterotetramer formation with Escherichia coli GAPDH reveals target for contraceptive design."
      Frayne J., Taylor A., Cameron G., Hadfield A.T.
      J. Biol. Chem. 284:22703-22712(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

    Entry informationi

    Entry nameiG3P1_ECOLI
    AccessioniPrimary (citable) accession number: P0A9B2
    Secondary accession number(s): P06977
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: March 16, 2016
    This is version 112 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.