UniProtKB - P10860 (DHE3_RAT)
Glutamate dehydrogenase 1, mitochondrial
Glud1
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 (By similarity).
Plays a role in insulin homeostasis (By similarity).
May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (PubMed:9275181).
By similarity1 PublicationCatalytic activityi
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 147 | SubstrateBy similarity | 1 | |
Binding sitei | 171 | SubstrateBy similarity | 1 | |
Binding sitei | 176 | NADBy similarity | 1 | |
Active sitei | 183 | PROSITE-ProRule annotation | 1 | |
Binding sitei | 252 | NADBy similarity | 1 | |
Binding sitei | 266 | GTPBy similarity | 1 | |
Binding sitei | 270 | GTPBy similarity | 1 | |
Binding sitei | 319 | GTPBy similarity | 1 | |
Binding sitei | 322 | GTPBy similarity | 1 | |
Binding sitei | 438 | SubstrateBy similarity | 1 | |
Binding sitei | 444 | NADBy similarity | 1 | |
Binding sitei | 450 | ADPBy similarity | 1 | |
Binding sitei | 516 | ADPBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 141 – 143 | NADBy similarity | 3 |
GO - Molecular functioni
- ADP binding Source: RGD
- ATP binding Source: UniProtKB-KW
- enzyme binding Source: RGD
- glutamate dehydrogenase (NAD+) activity Source: RGD
- glutamate dehydrogenase (NADP+) activity Source: RHEA
- glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB
- GTP binding Source: RGD
- leucine binding Source: RGD
- NAD+ binding Source: RGD
GO - Biological processi
- cerebellum development Source: RGD
- glutamate biosynthetic process Source: RGD
- glutamate catabolic process Source: RGD
- glutamine metabolic process Source: UniProtKB
- long-term memory Source: RGD
- positive regulation of insulin secretion Source: RGD
- response to aluminum ion Source: RGD
- tricarboxylic acid metabolic process Source: UniProtKB
Keywordsi
Molecular function | Oxidoreductase |
Ligand | ATP-binding, GTP-binding, NADP, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 1.4.1.3, 5301 |
Reactomei | R-RNO-2151201, Transcriptional activation of mitochondrial biogenesis R-RNO-8964539, Glutamate and glutamine metabolism |
SABIO-RKi | P10860 |
Names & Taxonomyi
Protein namesi | Recommended name: Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3By similarity)Short name: GDH 1 Alternative name(s): Memory-related gene 2 protein Short name: MRG-2 |
Gene namesi | Name:Glud1 Synonyms:Glud |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2708, Glud1 |
Subcellular locationi
Mitochondrion
- Mitochondrion By similarity
Endoplasmic reticulum
- Endoplasmic reticulum By similarity
Note: Mostly translocates into the mitochondria, only a small amount of the protein localizes to the endoplasmic reticulum.By similarity
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Mitochondrion
- mitochondrial matrix Source: RGD
- mitochondrion Source: RGD
Other locations
- cytoplasm Source: RGD
Keywords - Cellular componenti
Endoplasmic reticulum, MitochondrionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 53 | MitochondrionBy similarityAdd BLAST | 53 | |
ChainiPRO_0000007213 | 54 – 558 | Glutamate dehydrogenase 1, mitochondrialAdd BLAST | 505 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 68 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 79 | PhosphoserineCombined sources | 1 | |
Modified residuei | 84 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 84 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 90 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 110 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 110 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 128 | PhosphoserineCombined sources | 1 | |
Modified residuei | 135 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 147 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 162 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 162 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 171 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 172 | ADP-ribosylcysteineBy similarity | 1 | |
Modified residuei | 183 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 183 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 187 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 191 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 191 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 200 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 211 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 227 | PhosphoserineBy similarity | 1 | |
Modified residuei | 326 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 346 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 346 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 352 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 352 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 363 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 363 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 365 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 365 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 384 | PhosphoserineBy similarity | 1 | |
Modified residuei | 386 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 390 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 390 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 399 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 410 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 415 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 415 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 457 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 457 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 457 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 477 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 477 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 480 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 480 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 503 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 503 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 503 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 512 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 527 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 527 | N6-malonyllysine; alternateBy similarity | 1 | |
Modified residuei | 527 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 545 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 545 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 548 | N6-acetyllysineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, ADP-ribosylation, Hydroxylation, PhosphoproteinProteomic databases
jPOSTi | P10860 |
PaxDbi | P10860 |
PRIDEi | P10860 |
2D gel databases
World-2DPAGEi | 0004:P10860 |
PTM databases
CarbonylDBi | P10860 |
iPTMneti | P10860 |
PhosphoSitePlusi | P10860 |
Expressioni
Tissue specificityi
Inductioni
Gene expression databases
Bgeei | ENSRNOG00000057367, Expressed in liver and 22 other tissues |
Genevisiblei | P10860, RN |
Interactioni
Subunit structurei
Homohexamer (By similarity).
Interacts with HADH; this interaction inhibits the activation of GLUD1 (By similarity).
By similarityGO - Molecular functioni
- enzyme binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 246566, 3 interactors |
IntActi | P10860, 9 interactors |
MINTi | P10860 |
STRINGi | 10116.ENSRNOP00000013789 |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG2250, Eukaryota |
GeneTreei | ENSGT00390000000854 |
HOGENOMi | CLU_025763_1_0_1 |
InParanoidi | P10860 |
OMAi | PCFAAFP |
OrthoDBi | 692851at2759 |
PhylomeDBi | P10860 |
TreeFami | TF313945 |
Family and domain databases
CDDi | cd01076, NAD_bind_1_Glu_DH, 1 hit |
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 |
Pfami | View protein in Pfam PF00208, ELFV_dehydrog, 1 hit PF02812, ELFV_dehydrog_N, 1 hit |
PRINTSi | PR00082, GLFDHDRGNASE |
SMARTi | View protein in SMART SM00839, ELFV_dehydrog, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00074, GLFV_DEHYDROGENASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MYRRLGEVLL LSRAGPAALG SAAADSAALL GWARGQPSAV PQPGLTPVAR
60 70 80 90 100
RHYSEAATDR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRENEEQKRN
110 120 130 140 150
RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI
160 170 180 190 200
RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK
210 220 230 240 250
ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN
260 270 280 290 300
AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGLG
310 320 330 340 350
DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED
360 370 380 390 400
FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI
410 420 430 440 450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS
460 470 480 490 500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA
510 520 530 540 550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY
NEAGVTFT
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 56 – 57 | AA → GP in CAA32441 (PubMed:2704625).Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X14223 mRNA Translation: CAA32441.1 X14044 mRNA Translation: CAA32202.1 BC081841 mRNA Translation: AAH81841.1 X64365 Genomic DNA Translation: CAA45717.1 U95148 mRNA Translation: AAB70012.1 |
PIRi | S03707 |
RefSeqi | NP_036702.1, NM_012570.2 |
Genome annotation databases
Ensembli | ENSRNOT00000083446; ENSRNOP00000075032; ENSRNOG00000057367 |
GeneIDi | 24399 |
KEGGi | rno:24399 |
UCSCi | RGD:2708, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X14223 mRNA Translation: CAA32441.1 X14044 mRNA Translation: CAA32202.1 BC081841 mRNA Translation: AAH81841.1 X64365 Genomic DNA Translation: CAA45717.1 U95148 mRNA Translation: AAB70012.1 |
PIRi | S03707 |
RefSeqi | NP_036702.1, NM_012570.2 |
3D structure databases
SMRi | P10860 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 246566, 3 interactors |
IntActi | P10860, 9 interactors |
MINTi | P10860 |
STRINGi | 10116.ENSRNOP00000013789 |
Chemistry databases
ChEMBLi | CHEMBL2176833 |
PTM databases
CarbonylDBi | P10860 |
iPTMneti | P10860 |
PhosphoSitePlusi | P10860 |
2D gel databases
World-2DPAGEi | 0004:P10860 |
Proteomic databases
jPOSTi | P10860 |
PaxDbi | P10860 |
PRIDEi | P10860 |
Genome annotation databases
Ensembli | ENSRNOT00000083446; ENSRNOP00000075032; ENSRNOG00000057367 |
GeneIDi | 24399 |
KEGGi | rno:24399 |
UCSCi | RGD:2708, rat |
Organism-specific databases
CTDi | 2746 |
RGDi | 2708, Glud1 |
Phylogenomic databases
eggNOGi | KOG2250, Eukaryota |
GeneTreei | ENSGT00390000000854 |
HOGENOMi | CLU_025763_1_0_1 |
InParanoidi | P10860 |
OMAi | PCFAAFP |
OrthoDBi | 692851at2759 |
PhylomeDBi | P10860 |
TreeFami | TF313945 |
Enzyme and pathway databases
BRENDAi | 1.4.1.3, 5301 |
Reactomei | R-RNO-2151201, Transcriptional activation of mitochondrial biogenesis R-RNO-8964539, Glutamate and glutamine metabolism |
SABIO-RKi | P10860 |
Miscellaneous databases
PROi | PR:P10860 |
Gene expression databases
Bgeei | ENSRNOG00000057367, Expressed in liver and 22 other tissues |
Genevisiblei | P10860, RN |
Family and domain databases
CDDi | cd01076, NAD_bind_1_Glu_DH, 1 hit |
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 |
Pfami | View protein in Pfam PF00208, ELFV_dehydrog, 1 hit PF02812, ELFV_dehydrog_N, 1 hit |
PRINTSi | PR00082, GLFDHDRGNASE |
SMARTi | View protein in SMART SM00839, ELFV_dehydrog, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS00074, GLFV_DEHYDROGENASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | DHE3_RAT | |
Accessioni | P10860Primary (citable) accession number: P10860 Secondary accession number(s): Q66HI8, Q6LC16 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | April 4, 2006 | |
Last modified: | February 23, 2022 | |
This is version 182 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families