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P95544

- DHE4_PRERU

UniProt

P95544 - DHE4_PRERU

Protein

NAD(P)-specific glutamate dehydrogenase

Gene

gdhA

Organism
Prevotella ruminicola (Bacteroides ruminicola)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. P.ruminicola possess both NADP(H)- and NAD(H)-dependent activities on the same enzyme, suggesting that both anabolic and catabolic forms of the enzyme might occur.1 Publication

    Catalytic activityi

    L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation
    L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei88 – 881SubstrateBy similarity
    Binding sitei109 – 1091SubstrateBy similarity
    Binding sitei112 – 1121SubstrateBy similarity
    Active sitei124 – 1241Proton donorPROSITE-ProRule annotation
    Binding sitei163 – 1631Substrate; via carbonyl oxygenBy similarity
    Sitei164 – 1641Important for catalysisBy similarity
    Binding sitei207 – 2071NADPBy similarity
    Binding sitei238 – 2381NADPBy similarity
    Binding sitei376 – 3761SubstrateBy similarity

    GO - Molecular functioni

    1. glutamate dehydrogenase (NAD+) activity Source: UniProtKB-EC
    2. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB

    GO - Biological processi

    1. glutamate biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD(P)-specific glutamate dehydrogenase (EC:1.4.1.2, EC:1.4.1.3)
    Short name:
    NAD(P)-GDH
    Alternative name(s):
    NAD(P)H-dependent glutamate dehydrogenase
    Gene namesi
    Name:gdhA
    OrganismiPrevotella ruminicola (Bacteroides ruminicola)
    Taxonomic identifieri839 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPrevotellaceaePrevotella

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444NAD(P)-specific glutamate dehydrogenasePRO_0000182773Add
    BLAST

    Proteomic databases

    PRIDEiP95544.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP95544.
    SMRiP95544. Positions 3-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006095. Glu/Leu/Phe/Val_DH.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR014362. Glu_DH.
    IPR016040. NAD(P)-bd_dom.
    [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]
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P95544-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKATEVIEKL KAKFPGQPEY IQAVSQVLGT IEEEYNKHPE FEKANLIERL    50
    CVPDRILQFR VSWVDDNGNV QTNLGYRVQH NNAIGPYKGG LRFHKSVNAS 100
    ILKFLAFEQT FKNSLTTLPM GGAKGGSDFD PHGKSDMEVM RFCQAFMNEL 150
    YRLIGPDEDV PAGDIGVGGR EVGYMFGQYK KLTHQFQGIL TGKGLEFGGS 200
    LIRPEATGYG NVYFLEDMLK TRGESLEGKT VLVSGSGNVA QYTIEKLLQL 250
    GAKPVTCSDS NGYIYDPDGI DAEKLAFIME LKNVKRGRIK EYAEKYGVKY 300
    VENARPWGEK ADIATPCATQ DEINEAEAKT LIANGVFAVS EGANMPTEPA 350
    AIKVFQDAKI LYCPGKASNA GGVATSGLEM SQNSERLSWT REEVDTKLHN 400
    IMDEIHANCV KYGTEPDGYI NYVKGANVAG FMKVAKAMMA QGIY 444
    Length:444
    Mass (Da):48,878
    Last modified:May 1, 1997 - v1
    Checksum:i32CAD7F278CF06A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82240 Genomic DNA. Translation: AAB40142.1.
    PIRiT10487.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82240 Genomic DNA. Translation: AAB40142.1 .
    PIRi T10487.

    3D structure databases

    ProteinModelPortali P95544.
    SMRi P95544. Positions 3-444.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P95544.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR006095. Glu/Leu/Phe/Val_DH.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR014362. Glu_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000185. Glu_DH. 1 hit.
    PRINTSi PR00082. GLFDHDRGNASE.
    SMARTi SM00839. ELFV_dehydrog. 1 hit.
    [Graphical view ]
    PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The NAD(P)H-dependent glutamate dehydrogenase activities of Prevotella ruminicola B(1)4 can be attributed to one enzyme (GdhA), and gdhA expression is regulated in response to the nitrogen source available for growth."
      Wen Z., Morrison M.
      Appl. Environ. Microbiol. 62:3826-3833(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A GLUTAMATE DEHYDROGENASE, SUBSTRATE SPECIFICITY.
      Strain: B14.

    Entry informationi

    Entry nameiDHE4_PRERU
    AccessioniPrimary (citable) accession number: P95544
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3