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

    GO - Biological processi

    • cellular amino acid metabolic process Source: InterPro
    • glutamate biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:GDHA-MONOMER.
    ECOL316407:JW1750-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

    • cytoplasm Source: EcoliWiki
    • cytosol Source: EcoCyc
    Complete GO annotation...

    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-2DPAGEP00370.

    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.
    STRINGi511145.b1761.

    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-ray2.70A/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.
    OMAiVPWVDDA.
    PhylomeDBiP00370.

    Family and domain databases

    CDDicd05313. NAD_bind_2_Glu_DH. 1 hit.
    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006095. 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.
    IPR016040. NAD(P)-bd_dom.
    IPR033922. NAD_bind_Glu_DH.
    [Graphical view]
    PfamiPF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000185. Glu_DH. 1 hit.
    PRINTSiPR00082. GLFDHDRGNASE.
    SMARTiSM00839. ELFV_dehydrog. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]

    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.
    PATRICi32118833. VBIEscCol129921_1834.

    Cross-referencesi

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2YFHX-ray2.70A/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...

    Protein-protein interaction databases

    BioGridi4260322. 621 interactors.
    DIPiDIP-9756N.
    IntActiP00370. 1 interactor.
    STRINGi511145.b1761.

    2D gel databases

    SWISS-2DPAGEP00370.

    Proteomic databases

    EPDiP00370.
    PaxDbiP00370.
    PRIDEiP00370.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74831; AAC74831; b1761.
    BAA15550; BAA15550; BAA15550.
    GeneIDi946802.
    KEGGiecj:JW1750.
    eco:b1761.
    PATRICi32118833. VBIEscCol129921_1834.

    Organism-specific databases

    EchoBASEiEB0367.
    EcoGeneiEG10372. gdhA.

    Phylogenomic databases

    eggNOGiENOG4105D82. Bacteria.
    COG0334. LUCA.
    HOGENOMiHOG000243799.
    InParanoidiP00370.
    KOiK00262.
    OMAiVPWVDDA.
    PhylomeDBiP00370.

    Enzyme and pathway databases

    BioCyciEcoCyc:GDHA-MONOMER.
    ECOL316407:JW1750-MONOMER.
    MetaCyc:GDHA-MONOMER.
    BRENDAi1.4.1.4. 2026.

    Miscellaneous databases

    PROiP00370.

    Family and domain databases

    CDDicd05313. NAD_bind_2_Glu_DH. 1 hit.
    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006095. 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.
    IPR016040. NAD(P)-bd_dom.
    IPR033922. NAD_bind_Glu_DH.
    [Graphical view]
    PfamiPF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000185. Glu_DH. 1 hit.
    PRINTSiPR00082. GLFDHDRGNASE.
    SMARTiSM00839. ELFV_dehydrog. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDHE4_ECOLI
    AccessioniPrimary (citable) accession number: P00370
    Secondary accession number(s): P78173
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: November 30, 2016
    This is version 146 of the entry and version 1 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.