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Entry version 134 (26 Feb. 2020)
Sequence version 3 (28 Jul. 2009)
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Protein

Catabolic NAD-specific glutamate dehydrogenase RocG

Gene

rocG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.08 mM for NAD (at 37 degrees Celsius and at pH 7.3)2 Publications
  2. KM=0.34 mM for L-glutamate (at 37 degrees Celsius and at pH 7.3)2 Publications
  3. KM=2.9 mM for L-glutamate (at 37 degrees Celsius and at pH 7.3)2 Publications
  4. KM=0.65 mM for 2-oxoglutarate (at 37 degrees Celsius and at pH 7.3)2 Publications
  5. KM=2.9 mM for L-glutamate (at pH 7.3)2 Publications
  6. KM=18.5 mM for ammonium (at pH 7.7)2 Publications
  7. KM=55.6 mM for ammonium (at 37 degrees Celsius and at pH 7.3)2 Publications

    pH dependencei

    Optimum pH is 7.7 and 7.3 for L-glutamate deamination and 2-oxoglutarate amination, respectively. Half-maximal activity for deamination is observed at pH 6.9 and 7.8 and that for amination is at pH 6.9 and 7.8.2 Publications

    Temperature dependencei

    Low thermostability at 41 degrees Celsius due to the dissociation of the hexamer.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei80SubstrateBy similarity1
    Binding sitei104SubstrateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei116Proton donorPROSITE-ProRule annotation1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei156Important for catalysisBy similarity1
    Binding sitei200NADBy similarity1
    Binding sitei231NADBy similarity1
    Binding sitei358SubstrateBy similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    • glutamate dehydrogenase (NAD+) activity Source: UniProtKB

    GO - Biological processi

    • cellular amino acid metabolic process Source: UniProtKB
    • glutamate catabolic process Source: GO_Central
    • oxidation-reduction process Source: UniProtKB

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionOxidoreductase
    LigandNAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    BSUB:BSU37790-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.4.1.2 658

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P39633

    Protein family/group databases

    MoonProt database of moonlighting proteins

    More...
    MoonProti
    P39633

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Catabolic NAD-specific glutamate dehydrogenase RocG (EC:1.4.1.2)
    Short name:
    NAD-GDH
    Alternative name(s):
    Glutamate dehydrogenase
    Short name:
    GlutDH
    Trigger enzyme RocG
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:rocG
    Synonyms:gudA, yweB
    Ordered Locus Names:BSU37790
    ORF Names:ipa-75d
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus subtilis (strain 168)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri224308 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene lose the ability to utilize proline, ornithine, or arginine as sole carbon source and grow more slowly when proline or ornithine is utilized as sole nitrogen source.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi27E → F: Increase of thermostability 8 degrees Celsius higher than that of the wild-type. 1 Publication1
    Mutagenesisi93E → K: Reduces the affinity for glutamate and ammonium. 1 Publication1
    Mutagenesisi122D → N: Unable to control gltAB expression via an inhibitory interactions with the transcriptional regulator GltC. Reduces the affinity for glutamate and ammonium. 1 Publication1
    Mutagenesisi144Q → R: Increase of thermostability 20 degrees Celsius higher than that of the wild-type. 1 Publication1
    Mutagenesisi158Y → H: Reduces the affinity for glutamate and ammonium. 1 Publication1
    Mutagenesisi234S → R: Reduces the affinity for glutamate and ammonium. 1 Publication1
    Mutagenesisi324A → R: No effect. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001827351 – 424Catabolic NAD-specific glutamate dehydrogenase RocGAdd BLAST424

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P39633

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P39633

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P39633

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Expression depends on the alternative sigma-L factor and the transcription factor RocR. Induced by arginine, ornithine, or to a lesser extent proline. Repressed by glucose.3 Publications

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homohexamer.

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    P206682EBI-1642022,EBI-1642006

    Protein-protein interaction databases

    Protein interaction database and analysis system

    More...
    IntActi
    P39633, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    224308.BSU37790

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1424
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P39633

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P39633

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105D82 Bacteria
    COG0334 LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P39633

    KEGG Orthology (KO)

    More...
    KOi
    K00260

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    TNAWWWW

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P39633

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01076 NAD_bind_1_Glu_DH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View 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

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00208 ELFV_dehydrog, 1 hit
    PF02812 ELFV_dehydrog_N, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000185 Glu_DH, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00082 GLFDHDRGNASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00839 ELFV_dehydrog, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00074 GLFV_DEHYDROGENASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P39633-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSAKQVSKDE EKEALNLFLS TQTIIKEALR KLGYPGDMYE LMKEPQRMLT
    60 70 80 90 100
    VRIPVKMDNG SVKVFTGYRS QHNDAVGPTK GGVRFHPEVN EEEVKALSIW
    110 120 130 140 150
    MTLKCGIANL PYGGGKGGII CDPRTMSFGE LERLSRGYVR AISQIVGPTK
    160 170 180 190 200
    DIPAPDVYTN SQIMAWMMDE YSRLREFDSP GFITGKPLVL GGSQGRETAT
    210 220 230 240 250
    AQGVTICIEE AVKKKGIKLQ NARIIIQGFG NAGSFLAKFM HDAGAKVIGI
    260 270 280 290 300
    SDANGGLYNP DGLDIPYLLD KRDSFGMVTN LFTDVITNEE LLEKDCDILV
    310 320 330 340 350
    PAAISNQITA KNAHNIQASI VVEAANGPTT IDATKILNER GVLLVPDILA
    360 370 380 390 400
    SAGGVTVSYF EWVQNNQGYY WSEEEVAEKL RSVMVSSFET IYQTAATHKV
    410 420
    DMRLAAYMTG IRKSAEASRF RGWV
    Length:424
    Mass (Da):46,553
    Last modified:July 28, 2009 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i019AE0A833BE48DD
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti324A → R in CAA51631 (PubMed:7934828).Curated1
    Sequence conflicti419 – 424RFRGWV → FPRMGLI in CAA51631 (PubMed:7934828).Curated6

    <p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 46587 Da. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    X73124 Genomic DNA Translation: CAA51631.1
    AB194695 Genomic DNA Translation: BAD69594.1
    AL009126 Genomic DNA Translation: CAB15806.2
    S79622 Genomic DNA No translation available.

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A70055

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_391659.2, NC_000964.3
    WP_003227482.1, NZ_JNCM01000034.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CAB15806; CAB15806; BSU37790

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    937066

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bsu:BSU37790

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|224308.179.peg.4091

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X73124 Genomic DNA Translation: CAA51631.1
    AB194695 Genomic DNA Translation: BAD69594.1
    AL009126 Genomic DNA Translation: CAB15806.2
    S79622 Genomic DNA No translation available.
    PIRiA70055
    RefSeqiNP_391659.2, NC_000964.3
    WP_003227482.1, NZ_JNCM01000034.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3K92X-ray2.30A/B/C/D/E/F1-424[»]
    SMRiP39633
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    IntActiP39633, 1 interactor
    STRINGi224308.BSU37790

    Protein family/group databases

    MoonProtiP39633

    Proteomic databases

    jPOSTiP39633
    PaxDbiP39633
    PRIDEiP39633

    Genome annotation databases

    EnsemblBacteriaiCAB15806; CAB15806; BSU37790
    GeneIDi937066
    KEGGibsu:BSU37790
    PATRICifig|224308.179.peg.4091

    Phylogenomic databases

    eggNOGiENOG4105D82 Bacteria
    COG0334 LUCA
    InParanoidiP39633
    KOiK00260
    OMAiTNAWWWW
    PhylomeDBiP39633

    Enzyme and pathway databases

    BioCyciBSUB:BSU37790-MONOMER
    BRENDAi1.4.1.2 658
    SABIO-RKiP39633

    Miscellaneous databases

    EvolutionaryTraceiP39633

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDHE2_BACSU
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P39633
    Secondary accession number(s): Q53548, Q5W7E9
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 28, 2009
    Last modified: February 26, 2020
    This is version 134 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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