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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)DescriptionActionsGraphical viewLength
    Binding sitei34NAD3 Publications1
    Binding sitei78NAD; via carbonyl oxygen2 Publications1
    Binding sitei120NAD1 Publication1
    Active sitei150Nucleophile1 Publication1
    Sitei177Activates thiol group during catalysis1 Publication1
    Binding sitei180Glyceraldehyde 3-phosphateBy similarity1
    Binding sitei232Glyceraldehyde 3-phosphate1 Publication2 Publications1
    Binding sitei314NAD3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi12 – 13NAD4 Publications2

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    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)DescriptionActionsGraphical viewLength
    Mutagenesisi177H → N: Reduces activity about 50-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved2 Publications
    ChainiPRO_00001456482 – 331Glyceraldehyde-3-phosphate dehydrogenase AAdd BLAST330

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei115N6-succinyllysine1 Publication1
    Modified residuei124N6-succinyllysine1 Publication1
    Modified residuei132N6-acetyllysine; alternate1 Publication1
    Modified residuei132N6-succinyllysine; alternate1 Publication1
    Modified residuei138N6-acetyllysine1 Publication1
    Modified residuei192N6-acetyllysine; alternate1 Publication1
    Modified residuei192N6-succinyllysine; alternate1 Publication1
    Modified residuei213N6-succinyllysine1 Publication1
    Modified residuei217N6-succinyllysine1 Publication1
    Modified residuei225N6-succinyllysine1 Publication1
    Modified residuei249N6-acetyllysine1 Publication1
    Modified residuei249N6-succinyllysine1 Publication1
    Modified residuei257N6-succinyllysine1 Publication1
    Modified residuei261N6-succinyllysine1 Publication1
    Modified residuei331N6-malonyllysine; alternate1 Publication1
    Modified residuei331N6-succinyllysine; alternate1 Publication1

    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 interactors.
    851992. 1 interactor.
    DIPiDIP-31848N.
    IntActiP0A9B2. 25 interactors.
    MINTiMINT-1255410.
    STRINGi511145.b1779.

    Structurei

    Secondary structure

    1331
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 8Combined sources6
    Helixi12 – 22Combined sources11
    Beta strandi25 – 33Combined sources9
    Helixi38 – 46Combined sources9
    Turni49 – 51Combined sources3
    Beta strandi58 – 61Combined sources4
    Beta strandi64 – 67Combined sources4
    Beta strandi70 – 75Combined sources6
    Helixi80 – 83Combined sources4
    Helixi85 – 88Combined sources4
    Beta strandi91 – 95Combined sources5
    Beta strandi97 – 99Combined sources3
    Helixi103 – 106Combined sources4
    Helixi108 – 111Combined sources4
    Beta strandi115 – 121Combined sources7
    Beta strandi124 – 126Combined sources3
    Turni132 – 134Combined sources3
    Helixi136 – 138Combined sources3
    Beta strandi143 – 146Combined sources4
    Helixi150 – 166Combined sources17
    Beta strandi168 – 177Combined sources10
    Beta strandi183 – 187Combined sources5
    Helixi194 – 197Combined sources4
    Turni200 – 202Combined sources3
    Beta strandi205 – 208Combined sources4
    Turni211 – 214Combined sources4
    Helixi215 – 218Combined sources4
    Helixi220 – 222Combined sources3
    Beta strandi225 – 232Combined sources8
    Beta strandi239 – 249Combined sources11
    Helixi253 – 265Combined sources13
    Turni266 – 271Combined sources6
    Beta strandi272 – 275Combined sources4
    Helixi281 – 284Combined sources4
    Beta strandi289 – 294Combined sources6
    Turni295 – 297Combined sources3
    Beta strandi299 – 302Combined sources4
    Beta strandi305 – 312Combined sources8
    Helixi316 – 328Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A9B2.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni149 – 151Glyceraldehyde 3-phosphate binding1 Publication3
    Regioni209 – 210Glyceraldehyde 3-phosphate binding1 Publication2

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C17. Bacteria.
    COG0057. LUCA.
    HOGENOMiHOG000071678.
    InParanoidiP0A9B2.
    KOiK00134.
    OMAiKWGEVGA.
    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)DescriptionActionsGraphical viewLength
    Natural varianti43Y → I in strain: ECOR 70. 1
    Natural varianti266G → D in strain: E830587. 1
    Natural varianti267E → A in strain: E2666-74. 1

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260308. 24 interactors.
    851992. 1 interactor.
    DIPiDIP-31848N.
    IntActiP0A9B2. 25 interactors.
    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.
    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...

    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: November 2, 2016
    This is version 114 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.