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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Bos taurus (Bovine)
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

Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei147Substrate1 Publication1
Binding sitei171Substrate1 Publication1
Binding sitei176NAD1 Publication1
<p>This subsection of the ‘Function’ 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 sitei1831
Binding sitei252NAD1 Publication1
Binding sitei266GTP1 Publication1
Binding sitei270GTP1 Publication1
Binding sitei319GTP1 Publication1
Binding sitei322GTP1 Publication1
Binding sitei438Substrate1 Publication1
Binding sitei444NAD1 Publication1
Binding sitei450ADP1 Publication1
Binding sitei516ADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi141 – 143NAD1 Publication3

<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

GO - Biological processi

<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
LigandATP-binding, GTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.4.1.2 908

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00366

<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_and_taxonomy_section">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:
Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
Short name:
GDH 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:GLUD1
Synonyms:GLUD
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4628

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 57Mitochondrion1 PublicationAdd BLAST57
<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_000000720558 – 558Glutamate dehydrogenase 1, mitochondrialAdd BLAST501

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei68N6-succinyllysineBy similarity1
Modified residuei79PhosphoserineBy similarity1
Modified residuei84N6-acetyllysine; alternate1 Publication1
Modified residuei84N6-succinyllysine; alternate1 Publication1
Modified residuei90N6-acetyllysine1 Publication1
Modified residuei110N6-acetyllysine; alternate1 Publication1
Modified residuei110N6-succinyllysine; alternate1 Publication1
Modified residuei128PhosphoserineBy similarity1
Modified residuei135PhosphotyrosineBy similarity1
Modified residuei162N6-acetyllysine; alternate1 Publication1
Modified residuei162N6-succinyllysine; alternate1 Publication1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei172ADP-ribosylcysteineBy similarity1
Modified residuei183N6-acetyllysine; alternate1 Publication1
Modified residuei183N6-succinyllysine; alternateBy similarity1
Modified residuei187N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysine; alternate1 Publication1
Modified residuei191N6-succinyllysine; alternateBy similarity1
Modified residuei200N6-succinyllysineBy similarity1
Modified residuei211N6-acetyllysineBy similarity1
Modified residuei227PhosphoserineBy similarity1
Modified residuei326N6-acetyllysineBy similarity1
Modified residuei346N6-acetyllysine; alternateBy similarity1
Modified residuei346N6-succinyllysine; alternateBy similarity1
Modified residuei352N6-acetyllysine; alternateBy similarity1
Modified residuei352N6-succinyllysine; alternateBy similarity1
Modified residuei363N6-acetyllysine; alternate1 Publication1
Modified residuei363N6-succinyllysine; alternate1 Publication1
Modified residuei365N6-acetyllysine; alternate1 Publication1
Modified residuei365N6-succinyllysine; alternateBy similarity1
Modified residuei384PhosphoserineBy similarity1
Modified residuei386N6-acetyllysine1 Publication1
Modified residuei390N6-acetyllysine; alternateBy similarity1
Modified residuei390N6-succinyllysine; alternateBy similarity1
Modified residuei399N6-acetyllysine1 Publication1
Modified residuei410PhosphothreonineBy similarity1
Modified residuei415N6-acetyllysine; alternate1 Publication1
Modified residuei415N6-succinyllysine; alternate1 Publication1
Modified residuei457N6-acetyllysine; alternate1 Publication1
Modified residuei457N6-malonyllysine; alternate1 Publication1
Modified residuei457N6-succinyllysine; alternate1 Publication1
Modified residuei477N6-acetyllysine; alternateBy similarity1
Modified residuei477N6-succinyllysine; alternateBy similarity1
Modified residuei480N6-acetyllysine; alternate1 Publication1
Modified residuei480N6-succinyllysine; alternateBy similarity1
Modified residuei503N6-acetyllysine; alternate1 Publication1
Modified residuei503N6-malonyllysine; alternate1 Publication1
Modified residuei503N6-succinyllysine; alternate1 Publication1
Modified residuei512PhosphotyrosineBy similarity1
Modified residuei527N6-acetyllysine; alternate1 Publication1
Modified residuei527N6-malonyllysine; alternate1 Publication1
Modified residuei527N6-succinyllysine; alternate1 Publication1
Modified residuei545N6-acetyllysine; alternate1 Publication1
Modified residuei545N6-succinyllysine; alternate1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer (By similarity).By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P00366

PeptideAtlas

More...
PeptideAtlasi
P00366

PRoteomics IDEntifications database

More...
PRIDEi
P00366

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00366

<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_section">'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_section">'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_section%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
itself2EBI-1221442,EBI-1221442

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-39002N

Protein interaction database and analysis system

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IntActi
P00366, 1 interactor

Molecular INTeraction database

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MINTi
P00366

STRING: functional protein association networks

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STRINGi
9913.ENSBTAP00000009923

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P00366

<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

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HWYX-ray3.20A/B/C/D/E/F58-558[»]
1NQTX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L63-558[»]
1NR7X-ray3.30A/B/C/D/E/F/G/H/I/J/K/L63-558[»]
3ETDX-ray2.50A/B/C/D/E/F58-558[»]
3ETEX-ray3.00A/B/C/D/E/F58-558[»]
3ETGX-ray2.50A/B/C/D/E/F58-558[»]
3JCZelectron microscopy3.26A/B/C/D/E/F58-558[»]
3JD0electron microscopy3.47A/B/C/D/E/F58-558[»]
3JD1electron microscopy3.30A/B/C/D/E/F58-558[»]
3JD2electron microscopy3.30A/B/C/D/E/F58-558[»]
3JD3electron microscopy3.60A/B/C/D/E/F58-558[»]
3JD4electron microscopy3.40A/B/C/D/E/F58-558[»]
5K12electron microscopy1.80A/B/C/D/E/F1-558[»]
6DHDX-ray2.50A/B/C/D/E/F58-558[»]
6DHLX-ray3.62A/B/C/D/E/F58-558[»]
6DHMX-ray3.00A/B/C/D/E/F58-558[»]
6DHNX-ray3.30A/B/C/D/E/F58-558[»]
6DHQX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L58-558[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00366

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

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SMRi
P00366

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P00366

<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

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2250 Eukaryota
COG0334 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000243801

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005479

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00366

KEGG Orthology (KO)

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KOi
K00261

Database of Orthologous Groups

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OrthoDBi
692851at2759

TreeFam database of animal gene trees

More...
TreeFami
TF313945

Family and domain databases

Conserved Domains Database

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CDDi
cd01076 NAD_bind_1_Glu_DH, 1 hit

Integrated resource of protein families, domains and functional sites

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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
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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00082 GLFDHDRGNASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00839 ELFV_dehydrog, 1 hit

Superfamily database of structural and functional annotation

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P00366-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLVPPAR
60 70 80 90 100
RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRETEEQKRN
110 120 130 140 150
RVRSILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGVD VPAPDMSTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCITV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGTILG FPKAKIYEGS ILEVDCDILI PAASEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLNNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA
510 520 530 540 550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFRVY

NEAGVTFT
Length:558
Mass (Da):61,512
Last modified:September 13, 2004 - v2
<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:i194D74A33F2310E7
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 conflicti4Y → C in AAI03337 (Ref. 2) Curated1
Sequence conflicti14A → I in AAI03337 (Ref. 2) Curated1
Sequence conflicti22 – 23AS → VA in AAI03337 (Ref. 2) Curated2
Sequence conflicti28A → V in AAI03337 (Ref. 2) Curated1
Sequence conflicti32W → R in AAI03337 (Ref. 2) Curated1
Sequence conflicti37 – 38PA → AAAAV in AAI03337 (Ref. 2) Curated2
Sequence conflicti93 – 95ETE → QTQ AA sequence (PubMed:4735572).Curated3
Sequence conflicti104S → G in AAI03337 (Ref. 2) Curated1
Sequence conflicti104S → G AA sequence (PubMed:4735572).Curated1
Sequence conflicti141 – 142QH → HQ AA sequence (PubMed:4735572).Curated2
Sequence conflicti196 – 197NE → ED AA sequence (PubMed:4735572).Curated2
Sequence conflicti225D → N AA sequence (PubMed:4735572).Curated1
Sequence conflicti257 – 259GKP → KPG AA sequence (PubMed:4735572).Curated3
Sequence conflicti278 – 279HG → GH AA sequence (PubMed:4735572).Curated2
Sequence conflicti305V → A in AAI03337 (Ref. 2) Curated1
Sequence conflicti305V → A AA sequence (PubMed:4735572).Curated1
Sequence conflicti328I → V in AAI03337 (Ref. 2) Curated1
Sequence conflicti328I → V AA sequence (PubMed:4735572).Curated1
Sequence conflicti329T → A in AAI03337 (Ref. 2) Curated1
Sequence conflicti389T → P in AAP55683 (PubMed:14659072).Curated1
Sequence conflicti412E → Q AA sequence (PubMed:4735572).Curated1
Sequence conflicti441 – 442EW → QI AA sequence (PubMed:4735572).Curated2
Sequence conflicti444N → K in AAI03337 (Ref. 2) Curated1
Sequence conflicti444N → K AA sequence (PubMed:4735572).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY138843 mRNA Translation: AAN15276.1
AY256856 mRNA Translation: AAP55683.1
BC103336 mRNA Translation: AAI03337.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A92129 DEBOE

NCBI Reference Sequences

More...
RefSeqi
NP_872593.2, NM_182652.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Bt.107155
Bt.55415

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
281785

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:281785

<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
AY138843 mRNA Translation: AAN15276.1
AY256856 mRNA Translation: AAP55683.1
BC103336 mRNA Translation: AAI03337.1
PIRiA92129 DEBOE
RefSeqiNP_872593.2, NM_182652.2
UniGeneiBt.107155
Bt.55415

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HWYX-ray3.20A/B/C/D/E/F58-558[»]
1NQTX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L63-558[»]
1NR7X-ray3.30A/B/C/D/E/F/G/H/I/J/K/L63-558[»]
3ETDX-ray2.50A/B/C/D/E/F58-558[»]
3ETEX-ray3.00A/B/C/D/E/F58-558[»]
3ETGX-ray2.50A/B/C/D/E/F58-558[»]
3JCZelectron microscopy3.26A/B/C/D/E/F58-558[»]
3JD0electron microscopy3.47A/B/C/D/E/F58-558[»]
3JD1electron microscopy3.30A/B/C/D/E/F58-558[»]
3JD2electron microscopy3.30A/B/C/D/E/F58-558[»]
3JD3electron microscopy3.60A/B/C/D/E/F58-558[»]
3JD4electron microscopy3.40A/B/C/D/E/F58-558[»]
5K12electron microscopy1.80A/B/C/D/E/F1-558[»]
6DHDX-ray2.50A/B/C/D/E/F58-558[»]
6DHLX-ray3.62A/B/C/D/E/F58-558[»]
6DHMX-ray3.00A/B/C/D/E/F58-558[»]
6DHNX-ray3.30A/B/C/D/E/F58-558[»]
6DHQX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L58-558[»]
ProteinModelPortaliP00366
SMRiP00366
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39002N
IntActiP00366, 1 interactor
MINTiP00366
STRINGi9913.ENSBTAP00000009923

Chemistry databases

BindingDBiP00366
ChEMBLiCHEMBL4628

PTM databases

iPTMnetiP00366

Proteomic databases

PaxDbiP00366
PeptideAtlasiP00366
PRIDEiP00366

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281785
KEGGibta:281785

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2746

Phylogenomic databases

eggNOGiKOG2250 Eukaryota
COG0334 LUCA
HOGENOMiHOG000243801
HOVERGENiHBG005479
InParanoidiP00366
KOiK00261
OrthoDBi692851at2759
TreeFamiTF313945

Enzyme and pathway databases

BRENDAi1.4.1.2 908
SABIO-RKiP00366

Miscellaneous databases

EvolutionaryTraceiP00366

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
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
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...

<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 nameiDHE3_BOVIN
<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: P00366
Secondary accession number(s): Q3SYY0, Q7YS29, Q8HZ49
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 13, 2004
Last modified: January 16, 2019
This is version 154 of the entry and version 2 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 programChordata 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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