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. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).By similarity

Catalytic activityⁱ

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

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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	147	SubstrateBy similarity	1
Binding siteⁱ	171	SubstrateBy similarity	1
Binding siteⁱ	176	NADBy similarity	1
Active siteⁱ	183		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: BHF-UCL
Inferred from direct assayⁱ
- 12742085
ATP binding Source: UniProtKB-KW
glutamate dehydrogenase (NAD+) activity
Source: UniProtKB
Inferred from direct assayⁱ
- 15578726
glutamate dehydrogenase [NAD(P)+] activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 11032875
GTP binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 11032875
identical protein binding
Source: BHF-UCL
Traceable author statementⁱ
- 11903050
leucine binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 12742085
NAD+ binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 12193607

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular amino acid biosynthetic process Source: Reactome
glutamate biosynthetic process
Source: BHF-UCL
Inferred from direct assayⁱ
- 11032875
glutamate catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 6121377
glutamine metabolic process Source: UniProtKB
positive regulation of insulin secretion
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 11502802
substantia nigra development
Source: UniProtKB
Inferred from high throughput expression patternⁱ
- 22926577
tricarboxylic acid metabolic process Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	ATP-binding, GTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS07548-MONOMER
BRENDAⁱ	1.4.1.3 2681
Reactomeⁱ	R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis R-HSA-70614 Amino acid synthesis and interconversion (transamination)
SABIO-RKⁱ	P00367
SIGNORⁱ	P00367

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 10

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000148672.8
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4335 GLUD1
MIMⁱ	138130 gene
neXtProtⁱ	NX_P00367

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Familial hyperinsulinemic hypoglycemia 6 (HHF6)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionFamilial hyperinsulinemic hypoglycemia [MIM:256450], also referred to as congenital hyperinsulinism, nesidioblastosis, or persistent hyperinsulinemic hypoglycemia of infancy (PPHI), is the most common cause of persistent hypoglycemia in infancy and is due to defective negative feedback regulation of insulin secretion by low glucose levels. In HHF6 elevated oxidation rate of glutamate to alpha-ketoglutarate stimulates insulin secretion in the pancreatic beta cells, while they impair detoxification of ammonium in the liver.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	501	S → A: Reduces activity and inhibition by GTP. 1 Publication	1
Mutagenesisⁱ	507	H → A: Strongly reduces inhibition by GTP.	1
Mutagenesisⁱ	516	R → A: Abolishes activation by ADP. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	2746
GeneReviewsⁱ	GLUD1
MalaCards human disease database More...MalaCardsⁱ	GLUD1
MIMⁱ	606762 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000148672
Orphanetⁱ	35878 Hyperinsulinism-hyperammonemia syndrome
PharmGKBⁱ	PA28737

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB04137 Guanosine-5'-Triphosphate DB00756 Hexachlorophene DB00142 L-Glutamic Acid DB00157 NADH

DrugBankⁱ

DB04137 Guanosine-5'-Triphosphate
DB00756 Hexachlorophene
DB00142 L-Glutamic Acid
DB00157 NADH

Polymorphism and mutation databases

BioMutaⁱ	GLUD1
DMDMⁱ	118541

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 53	MitochondrionCombined sources2 PublicationsAdd BLAST		53
ChainⁱPRO_0000007206	54 – 558	Glutamate dehydrogenase 1, mitochondrialAdd BLAST		505

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	68	N6-succinyllysineBy similarity	1
Modified residueⁱ	79	PhosphoserineBy similarity	1
Modified residueⁱ	84	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	84	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	110	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	110	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	128	PhosphoserineBy similarity	1
Modified residueⁱ	135	PhosphotyrosineBy 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-ribosylcysteine1 Publication	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	PhosphoserineCombined sources	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	PhosphoserineCombined sources	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	PhosphothreonineBy similarity	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; alternateCombined sources	1
Modified residueⁱ	480	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	503	N6-acetyllysine; alternateCombined sources	1
Modified residueⁱ	503	N6-malonyllysine; alternateBy similarity	1
Modified residueⁱ	503	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	512	PhosphotyrosineCombined sources	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

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

Keywords - PTMⁱ

Acetylation, ADP-ribosylation, Phosphoprotein

Proteomic databases

EPDⁱ	P00367
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P00367
PaxDbⁱ	P00367
PeptideAtlas More...PeptideAtlasⁱ	P00367
PRIDEⁱ	P00367
ProteomicsDBⁱ	51236

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00016801
SWISS-2DPAGEⁱ	P00367
UCD-2DPAGEⁱ	P00367

PTM databases

iPTMnetⁱ	P00367
PhosphoSitePlusⁱ	P00367
SwissPalmⁱ	P00367

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000148672 Expressed in 228 organ(s), highest expression level in hypothalamus
CleanExⁱ	HS_GLUD1
ExpressionAtlasⁱ	P00367 baseline and differential
Genevisibleⁱ	P00367 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA042492 HPA044839 HPA061369

HPAⁱ

HPA042492
HPA044839
HPA061369

Interactionⁱ

Subunit structureⁱ

Homohexamer.

GO - Molecular functionⁱ

identical protein binding
Source: BHF-UCL
Traceable author statementⁱ
- 11903050

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109008, 43 interactors
IntActⁱ	P00367, 44 interactors
Molecular INTeraction database More...MINTⁱ	P00367
STRINGⁱ	9606.ENSP00000277865

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	66 – 90	Combined sources	25
Helixⁱ	91 – 93	Combined sources	3
Helixⁱ	95 – 97	Combined sources	3
Helixⁱ	99 – 102	Combined sources	4
Helixⁱ	104 – 109	Combined sources	6
Beta strandⁱ	113 – 123	Combined sources	11
Beta strandⁱ	125 – 127	Combined sources	3
Beta strandⁱ	129 – 138	Combined sources	10
Beta strandⁱ	142 – 152	Combined sources	11
Helixⁱ	158 – 174	Combined sources	17
Beta strandⁱ	180 – 186	Combined sources	7
Helixⁱ	190 – 192	Combined sources	3
Helixⁱ	195 – 211	Combined sources	17
Turnⁱ	217 – 219	Combined sources	3
Beta strandⁱ	220 – 223	Combined sources	4
Helixⁱ	230 – 242	Combined sources	13
Turnⁱ	243 – 247	Combined sources	5
Helixⁱ	251 – 253	Combined sources	3
Helixⁱ	260 – 262	Combined sources	3
Helixⁱ	271 – 284	Combined sources	14
Helixⁱ	287 – 293	Combined sources	7
Beta strandⁱ	298 – 300	Combined sources	3
Beta strandⁱ	303 – 307	Combined sources	5
Helixⁱ	311 – 322	Combined sources	12
Beta strandⁱ	326 – 331	Combined sources	6
Beta strandⁱ	336 – 338	Combined sources	3
Helixⁱ	345 – 354	Combined sources	10
Beta strandⁱ	355 – 358	Combined sources	4
Beta strandⁱ	364 – 366	Combined sources	3
Turnⁱ	371 – 373	Combined sources	3
Beta strandⁱ	377 – 381	Combined sources	5
Beta strandⁱ	383 – 386	Combined sources	4
Turnⁱ	390 – 392	Combined sources	3
Helixⁱ	393 – 395	Combined sources	3
Beta strandⁱ	399 – 402	Combined sources	4
Beta strandⁱ	405 – 407	Combined sources	3
Helixⁱ	411 – 419	Combined sources	9
Beta strandⁱ	423 – 425	Combined sources	3
Helixⁱ	427 – 430	Combined sources	4
Helixⁱ	433 – 447	Combined sources	15
Turnⁱ	451 – 455	Combined sources	5
Helixⁱ	456 – 475	Combined sources	20
Turnⁱ	476 – 479	Combined sources	4
Beta strandⁱ	481 – 483	Combined sources	3
Helixⁱ	491 – 498	Combined sources	8
Helixⁱ	502 – 527	Combined sources	26
Helixⁱ	534 – 551	Combined sources	18

Show more details

3D structure databases

ProteinModelPortalⁱ	P00367
SMRⁱ	P00367
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P00367

EvolutionaryTraceⁱ

P00367

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the Glu/Leu/Phe/Val dehydrogenases family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG2250 Eukaryota COG0334 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000000854
HOGENOMⁱ	HOG000243801
HOVERGENⁱ	HBG005479
InParanoidⁱ	P00367
KEGG Orthology (KO) More...KOⁱ	K00261
OMAⁱ	PCFAAFP
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0KMT
PhylomeDBⁱ	P00367
TreeFamⁱ	TF313945

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...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

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

Isoform 1 (identifier: P00367-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLALAAR 
        60         70         80         90        100
RHYSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN 
       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 SILGMTPGFG 
       310        320        330        340        350
DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED 
       360        370        380        390        400
FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI 
       410        420        430        440        450
IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS 
       460        470        480        490        500
YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA 
       510        520        530        540        550
SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY 

NEAGVTFT

Length:558

Mass (Da):61,398

Last modified:January 1, 1990 - v2

Checksum:ⁱA7319A840F57FBB2

GO

Isoform 2 (identifier: P00367-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-167: Missing.

« Hide

        10         20         30         40         50
MTYKCAVVDV PFGGAKAGVK INPKNYTDNE LEKITRRFTM ELAKKGFIGP 
        60         70         80         90        100
GIDVPAPDMS TGEREMSWIA DTYASTIGHY DINAHACVTG KPISQGGIHG 
       110        120        130        140        150
RISATGRGVF HGIENFINEA SYMSILGMTP GFGDKTFVVQ GFGNVGLHSM 
       160        170        180        190        200
RYLHRFGAKC IAVGESDGSI WNPDGIDPKE LEDFKLQHGS ILGFPKAKPY 
       210        220        230        240        250
EGSILEADCD ILIPAASEKQ LTKSNAPRVK AKIIAEGANG PTTPEADKIF 
       260        270        280        290        300
LERNIMVIPD LYLNAGGVTV SYFEWLKNLN HVSYGRLTFK YERDSNYHLL 
       310        320        330        340        350
MSVQESLERK FGKHGGTIPI VPTAEFQDRI SGASEKDIVH SGLAYTMERS 
       360        370        380        390 
ARQIMRTAMK YNLGLDLRTA AYVNAIEKVF KVYNEAGVTF T

Note: No experimental confirmation available.

Show »

Length:391

Mass (Da):42,950

Checksum:ⁱ8A493E2898605460

GO

Isoform 3 (identifier: P00367-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-16: MYRYLGEALLLSRAGP → MTCPCDNASSVFLGFC
17-149: Missing.

« Hide

        10         20         30         40         50
MTCPCDNASS VFLGFCIRYS TDVSVDEVKA LASLMTYKCA VVDVPFGGAK 
        60         70         80         90        100
AGVKINPKNY TDNELEKITR RFTMELAKKG FIGPGIDVPA PDMSTGEREM 
       110        120        130        140        150
SWIADTYAST IGHYDINAHA CVTGKPISQG GIHGRISATG RGVFHGIENF 
       160        170        180        190        200
INEASYMSIL GMTPGFGDKT FVVQGFGNVG LHSMRYLHRF GAKCIAVGES 
       210        220        230        240        250
DGSIWNPDGI DPKELEDFKL QHGSILGFPK AKPYEGSILE ADCDILIPAA 
       260        270        280        290        300
SEKQLTKSNA PRVKAKIIAE GANGPTTPEA DKIFLERNIM VIPDLYLNAG 
       310        320        330        340        350
GVTVSYFEWL KNLNHVSYGR LTFKYERDSN YHLLMSVQES LERKFGKHGG 
       360        370        380        390        400
TIPIVPTAEF QDRISGASEK DIVHSGLAYT MERSARQIMR TAMKYNLGLD 
       410        420 
LRTAAYVNAI EKVFKVYNEA GVTFT

Note: No experimental confirmation available.

Show »

Length:425

Mass (Da):46,575

Checksum:ⁱ2637B3023F58A7C4

GO

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_016760	270	S → C in HHF6; diminished sensitivity to GTP. 1 Publication	1
Natural variantⁱVAR_016761	274	R → C in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs56275071EnsemblClinVar.	1
Natural variantⁱVAR_009270	318	R → K in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909736EnsemblClinVar.	1
Natural variantⁱVAR_016762	318	R → T in HHF6; diminished sensitivity to GTP. 1 Publication	1
Natural variantⁱVAR_016763	319	Y → C in HHF6. 1 Publication	1
Natural variantⁱVAR_016764	322	R → C in HHF6; diminished sensitivity to GTP. 1 Publication	1
Natural variantⁱVAR_016765	322	R → H in HHF6; diminished sensitivity to GTP. 2 PublicationsCorresponds to variant dbSNP:rs121909737EnsemblClinVar.	1
Natural variantⁱVAR_009271	349	E → A in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909735EnsemblClinVar.	1
Natural variantⁱVAR_008666	498	S → L in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909731EnsemblClinVar.	1
Natural variantⁱVAR_008667	499	G → D in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909734EnsemblClinVar.	1
Natural variantⁱVAR_008668	499	G → S in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909733EnsemblClinVar.	1
Natural variantⁱVAR_008669	501	S → P in HHF6. 1 PublicationCorresponds to variant dbSNP:rs121909732EnsemblClinVar.	1
Natural variantⁱVAR_008670	507	H → Y in HHF6; abolishes inhibition by ATP; no effect on activation by ADP. 3 PublicationsCorresponds to variant dbSNP:rs121909730EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_056244	1 – 167	Missing in isoform 2. 1 PublicationAdd BLAST	167
Alternative sequenceⁱVSP_056523	1 – 16	MYRYL…SRAGP → MTCPCDNASSVFLGFC in isoform 3. 1 PublicationAdd BLAST	16
Alternative sequenceⁱVSP_056524	17 – 149	Missing in isoform 3. 1 PublicationAdd BLAST	133

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X07674 mRNA Translation: CAA30521.1 M20867 mRNA Translation: AAA52526.1 M37154 mRNA Translation: AAA52525.1 X07769 mRNA Translation: CAA30598.1 J03248 mRNA Translation: AAA52523.1 X66300 X66312 Genomic DNA Translation: CAA46994.2 AK122685 mRNA Translation: BAG53667.1 AK294685 mRNA Translation: BAG57846.1 AL136982 Genomic DNA Translation: CAI17120.1 CH471142 Genomic DNA Translation: EAW80300.1 CH471142 Genomic DNA Translation: EAW80302.1 BC040132 mRNA Translation: AAH40132.1 BC112946 mRNA Translation: AAI12947.1 X67491 Genomic DNA Translation: CAA47830.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS7382.1 [P00367-1]
PIRⁱ	A28208 DEHUE I37424 S29331 S60192
NCBI Reference Sequences More...RefSeqⁱ	NP_001305829.1, NM_001318900.1 [P00367-3] NP_001305830.1, NM_001318901.1 [P00367-2] NP_001305831.1, NM_001318902.1 [P00367-2] NP_001305833.1, NM_001318904.1 [P00367-2] NP_001305834.1, NM_001318905.1 [P00367-2] NP_001305835.1, NM_001318906.1 [P00367-2] NP_005262.1, NM_005271.4 [P00367-1]
UniGeneⁱ	Hs.500409 Hs.731740

Genome annotation databases

Ensemblⁱ	ENST00000277865; ENSP00000277865; ENSG00000148672 [P00367-1]
GeneIDⁱ	2746
KEGGⁱ	hsa:2746
UCSC genome browser More...UCSCⁱ	uc001keh.4 human [P00367-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P00367	Epididymis tissue sperm binding protein Li 18mP		HUMAN		558	UniRef100_P00367
Mitochondrial glutamate dehydrogenase 1 (Fragment)		PANTR		55
Mitochondrial glutamate dehydrogenase 1 (Fragment)		western gorilla		55

Protein	Similar proteins		Species	Score	Length	Source
P00367	Glutamate dehydrogenase 1, mitochondrial	)	BOVIN		558	UniRef90_P00367
Glutamate dehydrogenase 1, mitochondrial		MOUSE		558
Glutamate dehydrogenase 1, mitochondrial		RAT		558
Glutamate dehydrogenase 2, mitochondrial		HUMAN		558
Glutamate dehydrogenase 2, mitochondrial		PANTR		558
+176
P00367-3	Glutamate dehydrogenase		CAMFR		427	UniRef90_P00367-3
Glutamate dehydrogenase		MYOLU		425
UPI0004BD1D24		EQUPR		523
UPI0006712412		Anser cygnoides domesticus		419

Protein	Similar proteins		Species	Score	Length	Source
P00367	Glutamate dehydrogenase 1, mitochondrial		RAT		558	UniRef50_P00367
Glutamate dehydrogenase 2, mitochondrial		HUMAN		558
Glutamate dehydrogenase 2, mitochondrial		PANTR		558
Glutamate dehydrogenase 1, mitochondrial	)	BOVIN		558
Glutamate dehydrogenase 1, mitochondrial		MOUSE		558
+378
P00367-3	Glutamate dehydrogenase, mitochondrial		DROME		562	UniRef50_P00367-3
Glutamate dehydrogenase		CAMFR		427
Glutamate dehydrogenase		MYOLU		425
Glutamate dehydrogenase 1a		DANRE		544
Glutamate dehydrogenase 1		ONCMY		544
+555

Cross-referencesⁱ

Web resourcesⁱ

Wikipedia

Glutamate dehydrogenase 1 entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X07674 mRNA Translation: CAA30521.1 M20867 mRNA Translation: AAA52526.1 M37154 mRNA Translation: AAA52525.1 X07769 mRNA Translation: CAA30598.1 J03248 mRNA Translation: AAA52523.1 X66300 X66312 Genomic DNA Translation: CAA46994.2 AK122685 mRNA Translation: BAG53667.1 AK294685 mRNA Translation: BAG57846.1 AL136982 Genomic DNA Translation: CAI17120.1 CH471142 Genomic DNA Translation: EAW80300.1 CH471142 Genomic DNA Translation: EAW80302.1 BC040132 mRNA Translation: AAH40132.1 BC112946 mRNA Translation: AAI12947.1 X67491 Genomic DNA Translation: CAA47830.1
CCDSⁱ	CCDS7382.1 [P00367-1]
PIRⁱ	A28208 DEHUE I37424 S29331 S60192
RefSeqⁱ	NP_001305829.1, NM_001318900.1 [P00367-3] NP_001305830.1, NM_001318901.1 [P00367-2] NP_001305831.1, NM_001318902.1 [P00367-2] NP_001305833.1, NM_001318904.1 [P00367-2] NP_001305834.1, NM_001318905.1 [P00367-2] NP_001305835.1, NM_001318906.1 [P00367-2] NP_005262.1, NM_005271.4 [P00367-1]
UniGeneⁱ	Hs.500409 Hs.731740

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1L1F	X-ray	2.70	A/B/C/D/E/F	54-558	[»]
	1NR1	X-ray	3.30	A/B/C/D/E/F	63-558	[»]
	6DQG	X-ray	2.70	A/B/C/D/E/F	63-558	[»]
ProteinModelPortalⁱ	P00367
SMRⁱ	P00367
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109008, 43 interactors
IntActⁱ	P00367, 44 interactors
MINTⁱ	P00367
STRINGⁱ	9606.ENSP00000277865

Chemistry databases

DrugBankⁱ	DB04137 Guanosine-5'-Triphosphate DB00756 Hexachlorophene DB00142 L-Glutamic Acid DB00157 NADH

DrugBankⁱ

DB04137 Guanosine-5'-Triphosphate
DB00756 Hexachlorophene
DB00142 L-Glutamic Acid
DB00157 NADH

PTM databases

iPTMnetⁱ	P00367
PhosphoSitePlusⁱ	P00367
SwissPalmⁱ	P00367

Polymorphism and mutation databases

BioMutaⁱ	GLUD1
DMDMⁱ	118541

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00016801
SWISS-2DPAGEⁱ	P00367
UCD-2DPAGEⁱ	P00367

Proteomic databases

EPDⁱ	P00367
MaxQBⁱ	P00367
PaxDbⁱ	P00367
PeptideAtlasⁱ	P00367
PRIDEⁱ	P00367
ProteomicsDBⁱ	51236

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000277865; ENSP00000277865; ENSG00000148672 [P00367-1]
GeneIDⁱ	2746
KEGGⁱ	hsa:2746
UCSCⁱ	uc001keh.4 human [P00367-1]

Organism-specific databases

CTDⁱ	2746
DisGeNETⁱ	2746
EuPathDBⁱ	HostDB:ENSG00000148672.8
GeneCardsⁱ	GLUD1
GeneReviewsⁱ	GLUD1
HGNCⁱ	HGNC:4335 GLUD1
HPAⁱ	HPA042492 HPA044839 HPA061369
MalaCardsⁱ	GLUD1
MIMⁱ	138130 gene 606762 phenotype
neXtProtⁱ	NX_P00367
OpenTargetsⁱ	ENSG00000148672
Orphanetⁱ	35878 Hyperinsulinism-hyperammonemia syndrome
PharmGKBⁱ	PA28737
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2250 Eukaryota COG0334 LUCA
GeneTreeⁱ	ENSGT00390000000854
HOGENOMⁱ	HOG000243801
HOVERGENⁱ	HBG005479
InParanoidⁱ	P00367
KOⁱ	K00261
OMAⁱ	PCFAAFP
OrthoDBⁱ	EOG091G0KMT
PhylomeDBⁱ	P00367
TreeFamⁱ	TF313945

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS07548-MONOMER
BRENDAⁱ	1.4.1.3 2681
Reactomeⁱ	R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis R-HSA-70614 Amino acid synthesis and interconversion (transamination)
SABIO-RKⁱ	P00367
SIGNORⁱ	P00367

Miscellaneous databases

ChiTaRSⁱ	GLUD1 human
EvolutionaryTraceⁱ	P00367
GeneWikiⁱ	Glutamate_dehydrogenase_1
GenomeRNAiⁱ	2746
Protein Ontology More...PROⁱ	PR:P00367
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000148672 Expressed in 228 organ(s), highest expression level in hypothalamus
CleanExⁱ	HS_GLUD1
ExpressionAtlasⁱ	P00367 baseline and differential
Genevisibleⁱ	P00367 HS

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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DHE3_HUMAN
Accessionⁱ	P00367Primary (citable) accession number: P00367 Secondary accession number(s): B3KV55, B4DGN5, Q5TBU3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	January 1, 1990
	Last modified:	November 7, 2018
	This is version 211 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM

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UniProtKB - P00367 (DHE3_HUMAN)

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Glutamate dehydrogenase 1, mitochondrial

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<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

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GO - Biological processi

Enzyme and pathway databases

<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

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<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

Mitochondrion

Mitochondrion

Other locations

Keywords - Cellular componenti

<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

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Keywords - Diseasei

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Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

<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

3D structure databases

Miscellaneous databases

<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

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Alternative sequence

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Keywords - Coding sequence diversityi

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Sequence databases

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Protein-protein interaction databases

Chemistry databases

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Polymorphism and mutation databases

2D gel databases

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Protocols and materials databases

Genome annotation databases

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Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ