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Protein

NAD-specific glutamate dehydrogenase A

Gene

gdhX

Organism
Halobacterium salinarum (Halobacterium halobium)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Miscellaneous

Strain NRC-36014 contains 4 distinct glutamate dehydrogenases while strain NRC-1 contains only 3. GdhX is only present in strain NRC-36014 (PubMed:15780999).1 Publication

Caution

Was initially thought to be a NADP-specific glutamate dehydrogenase.1 Publication

Catalytic activityi

L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.2 Publications

Activity regulationi

Inhibited by ethanol, acetone, acetonitrile and 2-propanol (65 to 70% inhibition) and to a lesser extent by methanol and dimethyl formamide (26 and 49 % inhibition respectively). No effect of glycerol or DMSO.1 Publication

Kineticsi

kcat is 24 sec(-1) for glutamate in the presence of 3.2 M NaCl. kcat is 16 sec(-1) for NAD+ in the presence of 3.2 M NaCl. kcat is 56 sec(-1) for 2-oxoglutarate in the presence of 3.2 M NaCl. kcat is 85 sec(-1) for NH4+ in the presence of 3.2 M NaCl. kcat is 39 sec(-1) for NADH in the presence of 3.2 M NaCl. kcat is 17 sec(-1) for glutamate in the presence of 10% DMSO. kcat is 15 sec(-1) for NAD+ in the presence of 10% DMSO. kcat is 46 sec(-1) for 2-oxoglutarate in the presence of 20% DMSO. kcat is 84 sec(-1) for NH4+ in the presence of 20% DMSO. kcat is 47 sec(-1) for NADH in the presence of 20% DMSO.
  1. KM=14 mM for glutamate (for the recombinant enzyme, in the presence of 3.2 M NaCl)1 Publication
  2. KM=0.35 mM for NAD+ (for the recombinant enzyme, in the presence of 3.2 M NaCl)1 Publication
  3. KM=3.4 mM for 2-oxoglutarate (for the recombinant enzyme, in the presence of 3.2 M NaCl)1 Publication
  4. KM=118 mM for NH4+ (for the recombinant enzyme, in the presence of 3.2 M NaCl)1 Publication
  5. KM=0.011 mM for NADH (for the recombinant enzyme, in the presence of 3.2 M NaCl)1 Publication
  6. KM=9 mM for glutamate (for the recombinant enzyme, in the presence of 10% DMSO)1 Publication
  7. KM=0.13 mM for NAD+ (for the recombinant enzyme, in the presence of 10% DMSO)1 Publication
  8. KM=0.8 mM for 2-oxoglutarate (for the recombinant enzyme, in the presence of 20% DMSO)1 Publication
  9. KM=112 mM for NH4+ (for the recombinant enzyme, in the presence of 20% DMSO)1 Publication
  10. KM=0.025 mM for NADH (for the recombinant enzyme, in the presence of 20% DMSO)1 Publication

    pH dependencei

    Optimum pH for oxidative deamination is 9.2. Optimum pH for reductive amination is 8.5.1 Publication

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius. The enzyme is entirely stable from 50 to 70 degrees Celsius and 55 % activity is retained after 30 min at 90 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei126PROSITE-ProRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    LigandNAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-741
    BRENDAi1.4.1.2 2552

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD-specific glutamate dehydrogenase A (EC:1.4.1.2)
    Short name:
    NAD-GDH A
    Gene namesi
    Name:gdhX
    Synonyms:gdhA
    OrganismiHalobacterium salinarum (Halobacterium halobium)
    Taxonomic identifieri2242 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaStenosarchaea groupHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001827791 – 435NAD-specific glutamate dehydrogenase AAdd BLAST435

    Post-translational modificationi

    The N-terminus is blocked.1 Publication

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP29051
    SMRiP29051
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    CDDicd01076 NAD_bind_1_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.

    P29051-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTMASKSDST HDESGDEAAD STEPESALET ARRQLYHAAS YLDIDQNIVE
    60 70 80 90 100
    RLKYPKKVHE VTIPIERDDG TVEVFTGYRA QHDSVRGPYK GGLRYHPDVT
    110 120 130 140 150
    RDECVGLGMW MTWKCAVMDL PFGGAKGGVA VNPKELSPEE KERLTRRFTQ
    160 170 180 190 200
    EIRDVIGPNQ DIPAPDMGTD PQTMAWLMDA YSMQEGETTP GVVTGKPPVV
    210 220 230 240 250
    GGSEGREEAP GRSVAIITQL VCEYYDQPLD ETTVAVQGYG SVGANAARLL
    260 270 280 290 300
    DKWGATIVAI SDVNGAMYEP DGIDTASVPS HDEEPEAVTT YADTVISNEE
    310 320 330 340 350
    LLTLDVDVLI PAALGNVITK ENAEAIAADL VVEGANGPTT STADSILADR
    360 370 380 390 400
    DVAVIPDILA NAGGVTVSYF EWLQDINRRA WSLERVNDEL EAEMQAAWRA
    410 420 430
    VKDEYENRDV TWRDAAYIVA LSRIAEAHEA RGLWP
    Length:435
    Mass (Da):47,459
    Last modified:December 1, 1992 - v1
    Checksum:i0E4E940D2FF8B9D2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X63837 Genomic DNA Translation: CAA45327.1
    AY840088 Genomic DNA Translation: AAW19068.1
    PIRiS18609

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X63837 Genomic DNA Translation: CAA45327.1
    AY840088 Genomic DNA Translation: AAW19068.1
    PIRiS18609

    3D structure databases

    ProteinModelPortaliP29051
    SMRiP29051
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-741
    BRENDAi1.4.1.2 2552

    Family and domain databases

    CDDicd01076 NAD_bind_1_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
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDHE2_HALSI
    AccessioniPrimary (citable) accession number: P29051
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 10, 2018
    This is version 85 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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    Main funding by: National Institutes of Health

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