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Protein

NADP-specific glutamate dehydrogenase

Gene

gdhA

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

Functioni

Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.2 Publications

Catalytic activityi

L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH.

Enzyme regulationi

Competitively inhibited by homoserine and by glutamine.1 Publication

Kineticsi

  1. KM=40 µM for NADPH2 Publications
  2. KM=42 µM for NADP2 Publications
  3. KM=640 µM for 2-oxoglutarate2 Publications
  4. KM=1100 µM for ammonia2 Publications

    pH dependencei

    Optimum pH is 8 and 9 for the reductive amination and for the oxidative deamination, respectively. The enzyme remains active when heat treated or when left at room temperature for several months but is inactivated by freezing.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei92SubstrateBy similarity1
    Binding sitei113SubstrateBy similarity1
    Binding sitei116SubstrateBy similarity1
    Active sitei128Proton donorPROSITE-ProRule annotation1
    Binding sitei167Substrate; via carbonyl oxygenBy similarity1
    Sitei168Important for catalysis1
    Binding sitei211NADPBy similarity1
    Binding sitei242NADPBy similarity1
    Binding sitei380SubstrateBy similarity1

    GO - Molecular functioni

    • glutamate dehydrogenase (NADP+) activity Source: EcoCyc
    • identical protein binding Source: EcoCyc

    GO - Biological processi

    • glutamate biosynthetic process Source: EcoCyc

    Keywordsi

    Molecular functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BioCyciEcoCyc:GDHA-MONOMER
    MetaCyc:GDHA-MONOMER
    BRENDAi1.4.1.4 2026
    SABIO-RKiP00370

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADP-specific glutamate dehydrogenase (EC:1.4.1.4)
    Short name:
    NADP-GDH
    Gene namesi
    Name:gdhA
    Ordered Locus Names:b1761, JW1750
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10372 gdhA

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi92K → S: Complete loss of dehydrogenase activity. 1 Publication1
    Mutagenesisi128K → H: Reduces catalytic activity and increases pH optima for activity. Increases relative activity with amino acid substrates other than glutamate, especially L-norvaline. 1 Publication1
    Mutagenesisi128K → R: Reduced catalytic activity and increases pH optima for activity. NADP-specific glutamate dehydrogenase. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001827691 – 447NADP-specific glutamate dehydrogenaseAdd BLAST447

    Proteomic databases

    EPDiP00370
    PaxDbiP00370
    PRIDEiP00370

    2D gel databases

    SWISS-2DPAGEiP00370

    Expressioni

    Inductioni

    Induced by growth on glucose and ammonia.

    Interactioni

    Subunit structurei

    Homohexamer.2 Publications

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    BioGridi4260322, 628 interactors
    ComplexPortaliCPX-1976 glutamate dehydrogenase complex
    DIPiDIP-9756N
    IntActiP00370, 1 interactor
    MINTiP00370
    STRINGi316385.ECDH10B_1899

    Structurei

    Secondary structure

    1447
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi7 – 15Combined sources9
    Helixi22 – 41Combined sources20
    Helixi43 – 49Combined sources7
    Helixi50 – 54Combined sources5
    Beta strandi58 – 68Combined sources11
    Beta strandi74 – 85Combined sources12
    Beta strandi87 – 97Combined sources11
    Helixi103 – 119Combined sources17
    Beta strandi121 – 123Combined sources3
    Beta strandi126 – 132Combined sources7
    Helixi140 – 154Combined sources15
    Helixi155 – 157Combined sources3
    Turni160 – 162Combined sources3
    Beta strandi163 – 166Combined sources4
    Helixi173 – 187Combined sources15
    Helixi199 – 201Combined sources3
    Turni205 – 209Combined sources5
    Helixi210 – 225Combined sources16
    Beta strandi234 – 238Combined sources5
    Helixi242 – 253Combined sources12
    Beta strandi260 – 263Combined sources4
    Beta strandi266 – 269Combined sources4
    Helixi276 – 286Combined sources11
    Beta strandi288 – 290Combined sources3
    Helixi293 – 300Combined sources8
    Beta strandi303 – 306Combined sources4
    Helixi310 – 312Combined sources3
    Beta strandi316 – 320Combined sources5
    Helixi329 – 337Combined sources9
    Beta strandi342 – 344Combined sources3
    Beta strandi346 – 349Combined sources4
    Helixi353 – 361Combined sources9
    Beta strandi365 – 367Combined sources3
    Helixi369 – 372Combined sources4
    Helixi375 – 389Combined sources15
    Helixi395 – 415Combined sources21
    Beta strandi419 – 422Combined sources4
    Helixi425 – 443Combined sources19

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2YFHX-ray2.69A/B/C/D/E/F202-405[»]
    3SBOX-ray3.20A/B/C/D/E/F1-447[»]
    4BHTX-ray2.50A/B/C/D/E/F1-447[»]
    ProteinModelPortaliP00370
    SMRiP00370
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105D82 Bacteria
    COG0334 LUCA
    HOGENOMiHOG000243799
    InParanoidiP00370
    KOiK00262
    OMAiPCFAAFP
    PhylomeDBiP00370

    Family and domain databases

    CDDicd05313 NAD_bind_2_Glu_DH, 1 hit
    InterProiView protein in InterPro
    IPR006095 Glu/Leu/Phe/Val_DH
    IPR033524 Glu/Leu/Phe/Val_DH_AS
    IPR006096 Glu/Leu/Phe/Val_DH_C
    IPR006097 Glu/Leu/Phe/Val_DH_dimer_dom
    IPR014362 Glu_DH
    IPR036291 NAD(P)-bd_dom_sf
    IPR033922 NAD_bind_Glu_DH
    PfamiView protein in Pfam
    PF00208 ELFV_dehydrog, 1 hit
    PF02812 ELFV_dehydrog_N, 1 hit
    PIRSFiPIRSF000185 Glu_DH, 1 hit
    PRINTSiPR00082 GLFDHDRGNASE
    SMARTiView protein in SMART
    SM00839 ELFV_dehydrog, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    PROSITEiView protein in PROSITE
    PS00074 GLFV_DEHYDROGENASE, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P00370-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDQTYSLESF LNHVQKRDPN QTEFAQAVRE VMTTLWPFLE QNPKYRQMSL
    60 70 80 90 100
    LERLVEPERV IQFRVVWVDD RNQIQVNRAW RVQFSSAIGP YKGGMRFHPS
    110 120 130 140 150
    VNLSILKFLG FEQTFKNALT TLPMGGGKGG SDFDPKGKSE GEVMRFCQAL
    160 170 180 190 200
    MTELYRHLGA DTDVPAGDIG VGGREVGFMA GMMKKLSNNT ACVFTGKGLS
    210 220 230 240 250
    FGGSLIRPEA TGYGLVYFTE AMLKRHGMGF EGMRVSVSGS GNVAQYAIEK
    260 270 280 290 300
    AMEFGARVIT ASDSSGTVVD ESGFTKEKLA RLIEIKASRD GRVADYAKEF
    310 320 330 340 350
    GLVYLEGQQP WSLPVDIALP CATQNELDVD AAHQLIANGV KAVAEGANMP
    360 370 380 390 400
    TTIEATELFQ QAGVLFAPGK AANAGGVATS GLEMAQNAAR LGWKAEKVDA
    410 420 430 440
    RLHHIMLDIH HACVEHGGEG EQTNYVQGAN IAGFVKVADA MLAQGVI
    Length:447
    Mass (Da):48,581
    Last modified:July 21, 1986 - v1
    Checksum:i7CB861D282C533C6
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti385A → P in AAA23868 (PubMed:6373501).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J01615 Genomic DNA Translation: AAA87979.1
    K02499 Genomic DNA Translation: AAA23868.1
    U00096 Genomic DNA Translation: AAC74831.1
    AP009048 Genomic DNA Translation: BAA15550.1
    PIRiA00382 DEECEN
    RefSeqiNP_416275.1, NC_000913.3
    WP_000373021.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC74831; AAC74831; b1761
    BAA15550; BAA15550; BAA15550
    GeneIDi946802
    KEGGiecj:JW1750
    eco:b1761
    PATRICifig|1411691.4.peg.493

    Similar proteinsi

    Entry informationi

    Entry nameiDHE4_ECOLI
    AccessioniPrimary (citable) accession number: P00370
    Secondary accession number(s): P78173
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: June 20, 2018
    This is version 159 of the entry and version 1 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

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