Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glyceraldehyde-3-phosphate dehydrogenase A

Gene

gapA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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. 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

    Keywordsi

    Molecular functionOxidoreductase
    Biological processGlycolysis
    LigandNAD, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:GAPDH-A-MONOMER
    MetaCyc:GAPDH-A-MONOMER
    BRENDAi1.2.1.12 2026
    SABIO-RKiP0A9B2
    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: EcoCyc
    • membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi177H → N: Reduces activity about 50-fold. 1 Publication1

    Chemistry databases

    DrugBankiDB03814 2-(N-Morpholino)-Ethanesulfonic Acid
    DB02263 Glyceraldehyde-3-Phosphate

    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-2DPAGEiP0A9B2

    PTM databases

    iPTMnetiP0A9B2

    Interactioni

    Subunit structurei

    Homotetramer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    cheZP0A9H92EBI-368904,EBI-546726

    Protein-protein interaction databases

    BioGridi4260308, 65 interactors
    851992, 1 interactor
    DIPiDIP-31848N
    IntActiP0A9B2, 27 interactors
    MINTiP0A9B2
    STRINGi316385.ECDH10B_1917

    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
    OMAiFTLENMV
    PhylomeDBiP0A9B2

    Family and domain databases

    InterProiView protein in InterPro
    IPR020831 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
    IPR036291 NAD(P)-bd_dom_sf
    PANTHERiPTHR10836 PTHR10836, 1 hit
    PfamiView protein in Pfam
    PF02800 Gp_dh_C, 1 hit
    PF00044 Gp_dh_N, 1 hit
    PIRSFiPIRSF000149 GAP_DH, 1 hit
    PRINTSiPR00078 G3PDHDRGNASE
    SMARTiView protein in SMART
    SM00846 Gp_dh_N, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR01534 GAPDH-I, 1 hit
    PROSITEiView protein in PROSITE
    PS00071 GAPDH, 1 hit

    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
    PATRICifig|1411691.4.peg.475

    Entry informationi

    Entry nameiG3P1_ECOLI
    AccessioniPrimary (citable) accession number: P0A9B2
    Secondary accession number(s): P06977
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: March 28, 2018
    This is version 124 of the entry and version 2 of the sequence. See 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

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health