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P00366

- DHE3_BOVIN

UniProt

P00366 - DHE3_BOVIN

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Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

GLUD1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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. mitochondrion Source: AgBase
Complete GO annotation...

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.

Expressioni

Gene expression databases

ExpressionAtlasiP00366. baseline.

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

        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
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.

Gene expression databases

ExpressionAtlasi P00366. baseline.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 126 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