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Protein

NADP-specific glutamate dehydrogenase

Gene

gdhA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 sitei92SubstrateHMP:1
    Binding sitei113SubstrateHMP:1
    Binding sitei116SubstrateHMP:1
    Active sitei128Proton donorIEP:1
    Binding sitei167Substrate; via carbonyl oxygenHMP:1
    Sitei168Important for catalysis1
    Binding sitei211NADPHMP:1
    Binding sitei242NADPHMP:1
    Binding sitei380SubstrateHMP:1

    GO - Molecular functioni

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

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

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

    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

    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

    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. 621 interactors.
    DIPiDIP-9756N.
    IntActiP00370. 1 interactor.
    STRINGi316385.ECDH10B_1899.

    Structurei

    Secondary structure

    1447
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi7 – 15ND:9
    Helixi22 – 41ND:20
    Helixi43 – 49ND:7
    Helixi50 – 54ND:5
    Beta strandi58 – 68ND:11
    Beta strandi74 – 85ND:12
    Beta strandi87 – 97ND:11
    Helixi103 – 119ND:17
    Beta strandi121 – 123ND:3
    Beta strandi126 – 132ND:7
    Helixi140 – 154ND:15
    Helixi155 – 157ND:3
    Turni160 – 162ND:3
    Beta strandi163 – 166ND:4
    Helixi173 – 187ND:15
    Helixi199 – 201ND:3
    Turni205 – 209ND:5
    Helixi210 – 225ND:16
    Beta strandi234 – 238ND:5
    Helixi242 – 253ND:12
    Beta strandi260 – 263ND:4
    Beta strandi266 – 269ND:4
    Helixi276 – 286ND:11
    Beta strandi288 – 290ND:3
    Helixi293 – 300ND:8
    Beta strandi303 – 306ND:4
    Helixi310 – 312ND:3
    Beta strandi316 – 320ND:5
    Helixi329 – 337ND:9
    Beta strandi342 – 344ND:3
    Beta strandi346 – 349ND:4
    Helixi353 – 361ND:9
    Beta strandi365 – 367ND:3
    Helixi369 – 372ND:4
    Helixi375 – 389ND:15
    Helixi395 – 415ND:21
    Beta strandi419 – 422ND:4
    Helixi425 – 443ND:19

    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.
    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).IKR:1

    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: October 25, 2017
    This is version 155 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

    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