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P00366

- DHE3_BOVIN

UniProt

P00366 - DHE3_BOVIN

Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (13 Sep 2004)
      Previous versions | rss
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    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

    Catalytic activityi

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

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei147 – 1471Substrate1 Publication
    Binding sitei171 – 1711Substrate1 Publication
    Binding sitei176 – 1761NAD1 Publication
    Active sitei183 – 1831
    Binding sitei252 – 2521NAD1 Publication
    Binding sitei266 – 2661GTP1 Publication
    Binding sitei270 – 2701GTP1 Publication
    Binding sitei319 – 3191GTP1 Publication
    Binding sitei322 – 3221GTP1 Publication
    Binding sitei438 – 4381Substrate1 Publication
    Binding sitei444 – 4441NAD1 Publication
    Binding sitei450 – 4501ADP1 Publication
    Binding sitei516 – 5161ADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi141 – 1433NAD1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate dehydrogenase (NAD+) activity Source: AgBase
    3. glutamate dehydrogenase [NAD(P)+] activity Source: AgBase
    4. GTP binding Source: UniProtKB-KW

    GO - Biological processi

    1. glutamate catabolic process Source: AgBase
    2. glutamine metabolic process Source: UniProtKB
    3. positive regulation of insulin secretion Source: Ensembl
    4. tricarboxylic acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    ATP-binding, GTP-binding, NADP, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_217400. Amino acid synthesis and interconversion (transamination).
    SABIO-RKP00366.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH 1
    Gene namesi
    Name:GLUD1
    Synonyms:GLUD
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 28

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: AgBase
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: AgBase

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5757Mitochondrion1 PublicationAdd
    BLAST
    Chaini58 – 558501Glutamate dehydrogenase 1, mitochondrialPRO_0000007205Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681N6-succinyllysineBy similarity
    Modified residuei79 – 791PhosphoserineBy similarity
    Modified residuei84 – 841N6-acetyllysine; alternate1 Publication
    Modified residuei84 – 841N6-succinyllysine; alternate1 Publication
    Modified residuei90 – 901N6-acetyllysine1 Publication
    Modified residuei110 – 1101N6-acetyllysine; alternate1 Publication
    Modified residuei110 – 1101N6-succinyllysine; alternate1 Publication
    Modified residuei128 – 1281PhosphoserineBy similarity
    Modified residuei135 – 1351PhosphotyrosineBy similarity
    Modified residuei162 – 1621N6-acetyllysine; alternate1 Publication
    Modified residuei162 – 1621N6-succinyllysine; alternate1 Publication
    Modified residuei171 – 1711N6-acetyllysineBy similarity
    Modified residuei172 – 1721ADP-ribosylcysteineBy similarity
    Modified residuei183 – 1831N6-acetyllysine; alternate1 Publication
    Modified residuei183 – 1831N6-succinyllysine; alternateBy similarity
    Modified residuei187 – 1871N6-acetyllysineBy similarity
    Modified residuei191 – 1911N6-acetyllysine; alternate1 Publication
    Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
    Modified residuei200 – 2001N6-succinyllysineBy similarity
    Modified residuei211 – 2111N6-acetyllysineBy similarity
    Modified residuei326 – 3261N6-acetyllysineBy similarity
    Modified residuei346 – 3461N6-acetyllysine; alternateBy similarity
    Modified residuei346 – 3461N6-succinyllysine; alternateBy similarity
    Modified residuei352 – 3521N6-acetyllysine; alternateBy similarity
    Modified residuei352 – 3521N6-succinyllysine; alternateBy similarity
    Modified residuei363 – 3631N6-acetyllysine; alternate1 Publication
    Modified residuei363 – 3631N6-succinyllysine; alternate1 Publication
    Modified residuei365 – 3651N6-acetyllysine; alternate1 Publication
    Modified residuei365 – 3651N6-succinyllysine; alternateBy similarity
    Modified residuei386 – 3861N6-acetyllysine1 Publication
    Modified residuei390 – 3901N6-acetyllysine; alternateBy similarity
    Modified residuei390 – 3901N6-succinyllysine; alternateBy similarity
    Modified residuei399 – 3991N6-acetyllysine1 Publication
    Modified residuei415 – 4151N6-acetyllysine; alternate1 Publication
    Modified residuei415 – 4151N6-succinyllysine; alternate1 Publication
    Modified residuei457 – 4571N6-acetyllysine; alternate1 Publication
    Modified residuei457 – 4571N6-malonyllysine; alternate1 Publication
    Modified residuei457 – 4571N6-succinyllysine; alternate1 Publication
    Modified residuei477 – 4771N6-acetyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-succinyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
    Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-acetyllysine; alternate1 Publication
    Modified residuei503 – 5031N6-malonyllysine; alternate1 Publication
    Modified residuei503 – 5031N6-succinyllysine; alternate1 Publication
    Modified residuei527 – 5271N6-acetyllysine; alternate1 Publication
    Modified residuei527 – 5271N6-malonyllysine; alternate1 Publication
    Modified residuei527 – 5271N6-succinyllysine; alternate1 Publication
    Modified residuei545 – 5451N6-acetyllysine; alternate1 Publication
    Modified residuei545 – 5451N6-succinyllysine; alternate1 Publication

    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

    PaxDbiP00366.
    PRIDEiP00366.

    Interactioni

    Subunit structurei

    Homohexamer.2 Publications

    Protein-protein interaction databases

    DIPiDIP-39002N.
    IntActiP00366. 1 interaction.

    Structurei

    Secondary structure

    1
    558
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi60 – 623
    Helixi66 – 8823
    Helixi97 – 10913
    Beta strandi113 – 12311
    Beta strandi125 – 1273
    Beta strandi129 – 13810
    Beta strandi142 – 1476
    Beta strandi150 – 1523
    Helixi158 – 17417
    Beta strandi180 – 1867
    Helixi190 – 1923
    Helixi195 – 21117
    Beta strandi214 – 2163
    Turni217 – 2193
    Beta strandi220 – 2234
    Helixi230 – 24213
    Turni243 – 2475
    Helixi251 – 2533
    Beta strandi255 – 2573
    Helixi260 – 2623
    Turni266 – 2705
    Helixi271 – 28414
    Helixi287 – 2926
    Beta strandi297 – 2993
    Beta strandi303 – 3075
    Helixi311 – 32212
    Beta strandi326 – 3316
    Beta strandi336 – 3383
    Helixi345 – 35511
    Beta strandi356 – 3583
    Beta strandi364 – 3674
    Helixi371 – 3733
    Beta strandi377 – 3815
    Beta strandi383 – 3853
    Turni390 – 3923
    Helixi393 – 3953
    Beta strandi399 – 4024
    Beta strandi405 – 4073
    Helixi411 – 4199
    Beta strandi423 – 4253
    Helixi427 – 4304
    Helixi433 – 44715
    Turni451 – 4555
    Helixi456 – 47722
    Turni480 – 4823
    Helixi491 – 4966
    Helixi502 – 52726
    Helixi534 – 55219
    Turni554 – 5563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HWYX-ray3.20A/B/C/D/E/F58-558[»]
    1HWZX-ray2.80A/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[»]
    3MVOX-ray3.23A/B/C/D/E/F58-558[»]
    3MVQX-ray2.94A/B/C/D/E/F58-558[»]
    3MW9X-ray2.50A/B/C/D/E/F58-558[»]
    3QMUX-ray3.62A/B/C/D/E/F/G/H/I/J/K/L58-558[»]
    ProteinModelPortaliP00366.
    SMRiP00366. Positions 63-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00366.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0334.
    GeneTreeiENSGT00390000000854.
    HOGENOMiHOG000243801.
    HOVERGENiHBG005479.
    InParanoidiP00366.
    KOiK00261.
    OrthoDBiEOG73NG50.
    TreeFamiTF313945.

    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.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    PRINTSiPR00082. GLFDHDRGNASE.
    SMARTiSM00839. ELFV_dehydrog. 1 hit.
    [Graphical view]
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00366-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLVPPAR    50
    RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRETEEQKRN 100
    RVRSILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 150
    RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK 200
    ITRRFTMELA KKGFIGPGVD VPAPDMSTGE REMSWIADTY ASTIGHYDIN 250
    AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 300
    DKTFVVQGFG NVGLHSMRYL HRFGAKCITV GESDGSIWNP DGIDPKELED 350
    FKLQHGTILG FPKAKIYEGS ILEVDCDILI PAASEKQLTK SNAPRVKAKI 400
    IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLNNLNHVS 450
    YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA 500
    SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFRVY 550
    NEAGVTFT 558
    Length:558
    Mass (Da):61,512
    Last modified:September 13, 2004 - v2
    Checksum:i194D74A33F2310E7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41Y → C in AAI03337. 1 PublicationCurated
    Sequence conflicti14 – 141A → I in AAI03337. 1 PublicationCurated
    Sequence conflicti22 – 232AS → VA in AAI03337. 1 PublicationCurated
    Sequence conflicti28 – 281A → V in AAI03337. 1 PublicationCurated
    Sequence conflicti32 – 321W → R in AAI03337. 1 PublicationCurated
    Sequence conflicti37 – 382PA → AAAAV in AAI03337. 1 PublicationCurated
    Sequence conflicti93 – 953ETE → QTQ AA sequence (PubMed:4735572)Curated
    Sequence conflicti104 – 1041S → G in AAI03337. 1 PublicationCurated
    Sequence conflicti104 – 1041S → G AA sequence (PubMed:4735572)Curated
    Sequence conflicti141 – 1422QH → HQ AA sequence (PubMed:4735572)Curated
    Sequence conflicti196 – 1972NE → ED AA sequence (PubMed:4735572)Curated
    Sequence conflicti225 – 2251D → N AA sequence (PubMed:4735572)Curated
    Sequence conflicti257 – 2593GKP → KPG AA sequence (PubMed:4735572)Curated
    Sequence conflicti278 – 2792HG → GH AA sequence (PubMed:4735572)Curated
    Sequence conflicti305 – 3051V → A in AAI03337. 1 PublicationCurated
    Sequence conflicti305 – 3051V → A AA sequence (PubMed:4735572)Curated
    Sequence conflicti328 – 3281I → V in AAI03337. 1 PublicationCurated
    Sequence conflicti328 – 3281I → V AA sequence (PubMed:4735572)Curated
    Sequence conflicti329 – 3291T → A in AAI03337. 1 PublicationCurated
    Sequence conflicti389 – 3891T → P in AAP55683. (PubMed:14659072)Curated
    Sequence conflicti412 – 4121E → Q AA sequence (PubMed:4735572)Curated
    Sequence conflicti441 – 4422EW → QI AA sequence (PubMed:4735572)Curated
    Sequence conflicti444 – 4441N → K in AAI03337. 1 PublicationCurated
    Sequence conflicti444 – 4441N → K AA sequence (PubMed:4735572)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY138843 mRNA. Translation: AAN15276.1.
    AY256856 mRNA. Translation: AAP55683.1.
    BC103336 mRNA. Translation: AAI03337.1.
    PIRiA92129. DEBOE.
    RefSeqiNP_872593.1. NM_182652.1.
    UniGeneiBt.107155.

    Genome annotation databases

    EnsembliENSBTAT00000009923; ENSBTAP00000009923; ENSBTAG00000007540.
    GeneIDi281785.
    KEGGibta:281785.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY138843 mRNA. Translation: AAN15276.1 .
    AY256856 mRNA. Translation: AAP55683.1 .
    BC103336 mRNA. Translation: AAI03337.1 .
    PIRi A92129. DEBOE.
    RefSeqi NP_872593.1. NM_182652.1.
    UniGenei Bt.107155.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HWY X-ray 3.20 A/B/C/D/E/F 58-558 [» ]
    1HWZ X-ray 2.80 A/B/C/D/E/F 58-558 [» ]
    1NQT X-ray 3.50 A/B/C/D/E/F/G/H/I/J/K/L 63-558 [» ]
    1NR7 X-ray 3.30 A/B/C/D/E/F/G/H/I/J/K/L 63-558 [» ]
    3ETD X-ray 2.50 A/B/C/D/E/F 58-558 [» ]
    3ETE X-ray 3.00 A/B/C/D/E/F 58-558 [» ]
    3ETG X-ray 2.50 A/B/C/D/E/F 58-558 [» ]
    3MVO X-ray 3.23 A/B/C/D/E/F 58-558 [» ]
    3MVQ X-ray 2.94 A/B/C/D/E/F 58-558 [» ]
    3MW9 X-ray 2.50 A/B/C/D/E/F 58-558 [» ]
    3QMU X-ray 3.62 A/B/C/D/E/F/G/H/I/J/K/L 58-558 [» ]
    ProteinModelPortali P00366.
    SMRi P00366. Positions 63-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-39002N.
    IntActi P00366. 1 interaction.

    Chemistry

    BindingDBi P00366.
    ChEMBLi CHEMBL4628.

    Proteomic databases

    PaxDbi P00366.
    PRIDEi P00366.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000009923 ; ENSBTAP00000009923 ; ENSBTAG00000007540 .
    GeneIDi 281785.
    KEGGi bta:281785.

    Organism-specific databases

    CTDi 2746.

    Phylogenomic databases

    eggNOGi COG0334.
    GeneTreei ENSGT00390000000854.
    HOGENOMi HOG000243801.
    HOVERGENi HBG005479.
    InParanoidi P00366.
    KOi K00261.
    OrthoDBi EOG73NG50.
    TreeFami TF313945.

    Enzyme and pathway databases

    Reactomei REACT_217400. Amino acid synthesis and interconversion (transamination).
    SABIO-RK P00366.

    Miscellaneous databases

    EvolutionaryTracei P00366.
    NextBioi 20805698.

    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.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00082. GLFDHDRGNASE.
    SMARTi SM00839. ELFV_dehydrog. 1 hit.
    [Graphical view ]
    PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase."
      Kim D.W., Eum W.S., Jang S.H., Yoon C.S., Kim Y.H., Choi S.H., Choi H.S., Kim S.Y., Kwon H.Y., Kang J.H., Kwon O.-S., Cho S.-W., Park J., Choi S.Y.
      J. Biochem. Mol. Biol. 36:545-551(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ALLOSTERIC REGULATION.
      Tissue: Brain.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.
    3. "Sequence of bovine liver glutamate dehydrogenase. 8. Peptides produced by specific chemical cleavages; the complete sequence of the protein."
      Moon K., Smith E.L.
      J. Biol. Chem. 248:3082-3088(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 58-558.
      Tissue: Liver.
    4. "Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme."
      Julliard J.H., Smith E.L.
      J. Biol. Chem. 254:3427-3438(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 440-441.
    5. "Studies of glutamate dehydrogenase: chemical modification and quantitative determination of tryptophan residues."
      Witzemann V., Koberstein R., Sund H., Rasched I., Joernvall H., Noack K.
      Eur. J. Biochem. 43:319-325(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "Studies of glutamate dehydrogenase. Identification of an amino group involved in the substrate binding."
      Rasched I., Joernvall H., Sund H.
      Eur. J. Biochem. 41:603-606(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY STUDIES OF SUBSTRATE-BINDING SITE.
    7. "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."
      Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., Hao Q., Lin H.
      Science 334:806-809(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-84; LYS-90; LYS-110; LYS-162; LYS-183; LYS-191; LYS-363; LYS-365; LYS-386; LYS-399; LYS-415; LYS-457; LYS-480; LYS-503; LYS-527 AND LYS-545, MALONYLATION AT LYS-457; LYS-503 AND LYS-527, SUCCINYLATION AT LYS-84; LYS-110; LYS-162; LYS-363; LYS-415; LYS-457; LYS-503; LYS-527 AND LYS-545.
    8. "The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery."
      Peterson P.E., Smith T.J.
      Structure 7:769-782(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558.
      Tissue: Liver.
    9. "Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation."
      Smith T.J., Peterson P.E., Schmidt T., Fang J., Stanley C.A.
      J. Mol. Biol. 307:707-720(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558 IN COMPLEX WITH SUBSTRATE; NADH AND GTP, FUNCTION.
    10. "Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation."
      Banerjee S., Schmidt T., Fang J., Stanley C.A., Smith T.J.
      Biochemistry 42:3446-3456(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 25-520 ALONE AND IN COMPLEX WITH ADP, HOMOHEXAMERIZATION.

    Entry informationi

    Entry nameiDHE3_BOVIN
    AccessioniPrimary (citable) accession number: P00366
    Secondary accession number(s): Q3SYY0, Q7YS29, Q8HZ49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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

    External Data

    Dasty 3