Hmdb loader
Identification
HMDB Protein ID HMDBP00694
Secondary Accession Numbers
  • 5967
  • HMDBP03650
Name Glutamate dehydrogenase 1, mitochondrial
Synonyms
  1. GDH 1
Gene Name GLUD1
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity).
Pathways
  • 2-Hydroxyglutric Aciduria (D And L Form)
  • 4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase Deficiency
  • Alanine, aspartate and glutamate metabolism
  • Arginine and proline metabolism
  • Arginine and proline metabolism
  • Arginine: Glycine Amidinotransferase Deficiency (AGAT Deficiency)
  • Argininemia
  • Argininosuccinic Aciduria
  • Carbamoyl Phosphate Synthetase Deficiency
  • Citrullinemia Type I
  • Creatine deficiency, guanidinoacetate methyltransferase deficiency
  • D-Glutamine and D-glutamate metabolism
  • Glucose-Alanine Cycle
  • Glutamate Metabolism
  • Glutaminolysis and Cancer
  • Guanidinoacetate Methyltransferase Deficiency (GAMT Deficiency)
  • Homocarnosinosis
  • Hyperinsulinism-Hyperammonemia Syndrome
  • Hyperornithinemia with gyrate atrophy (HOGA)
  • Hyperornithinemia-hyperammonemia-homocitrullinuria [HHH-syndrome]
  • Hyperprolinemia Type I
  • Hyperprolinemia Type II
  • L-arginine:glycine amidinotransferase deficiency
  • Nitrogen metabolism
  • Ornithine Aminotransferase Deficiency (OAT Deficiency)
  • Ornithine Transcarbamylase Deficiency (OTC Deficiency)
  • Prolidase Deficiency (PD)
  • Prolinemia Type II
  • Proximal tubule bicarbonate reclamation
  • Succinic semialdehyde dehydrogenase deficiency
  • The oncogenic action of D-2-hydroxyglutarate in Hydroxygluaricaciduria
  • The oncogenic action of L-2-hydroxyglutarate in Hydroxygluaricaciduria
  • Urea Cycle
  • Warburg Effect
Reactions
L-Glutamic acid + Water + NAD(P)(+) → Oxoglutaric acid + Ammonia + NAD(P)H details
L-Glutamic acid + NAD + Water → Oxoglutaric acid + Ammonia + NADH + Hydrogen Ion details
L-Glutamic acid + NADP + Water → Oxoglutaric acid + Ammonia + NADPH + Hydrogen Ion details
GO Classification
Biological Process
cellular nitrogen compound metabolic process
positive regulation of insulin secretion
glutamate biosynthetic process
glutamate catabolic process
Cellular Component
mitochondrial matrix
Function
binding
catalytic activity
oxidoreductase activity
Molecular Function
ATP binding
GTP binding
ADP binding
glutamate dehydrogenase (NAD+) activity
glutamate dehydrogenase [NAD(P)+] activity
leucine binding
NAD+ binding
identical protein binding
Process
metabolic process
cellular metabolic process
oxidation reduction
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Cellular Location
  1. Mitochondrion matrix
Gene Properties
Chromosome Location 10
Locus 10q23.3
SNPs GLUD1
Gene Sequence
>1677 bp
ATGTACCGCTACCTGGGCGAAGCGCTGTTGCTGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCGGCGTCCGCCGACTCGGCCGCGTTGCTGGGCTGGGCCCGGGGACAGCCCGCCGCCGCC
CCGCAGCCGGGGCTGGCATTGGCCGCCCGGCGCCACTACAGCGAGGCGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGCTGGTGGAGGACCTGAGGACCCGGGAGAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACTGATAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAAAAGGGCTTTATTGGTCCTGGCATTGAT
GTGCCTGCTCCAGACATGAGCACAGGTGAGCGGGAGATGTCCTGGATCGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAATTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTGGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGCCGACTGTGACATACTGATC
CCAGCTGCCAGTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGACAAGATCTTCCTGGAGAGA
AACATTATGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCATGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGGATATCGGGTGCA
TCTGAGAAAGACATCGTGCACTCTGGCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCGCACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTT
AATGCCATTGAGAAAGTCTTCAAAGTGTACAATGAAGCTGGTGTGACCTTCACATAG
Protein Properties
Number of Residues 558
Molecular Weight 61397.315
Theoretical pI 7.803
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glutamate dehydrogenase 1, mitochondrial
MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADR
EDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFG
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGK
HGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYV
NAIEKVFKVYNEAGVTFT
GenBank ID Protein 31707
UniProtKB/Swiss-Prot ID P00367
UniProtKB/Swiss-Prot Entry Name DHE3_HUMAN
PDB IDs
GenBank Gene ID X07674
GeneCard ID GLUD1
GenAtlas ID GLUD1
HGNC ID HGNC:4335
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed:1286669 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed:15164054 ]
  7. Nakatani Y, Banner C, von Herrath M, Schneider ME, Smith HH, Freese E: Comparison of human brain and liver glutamate dehydrogenase cDNAS. Biochem Biophys Res Commun. 1987 Dec 16;149(2):405-10. [PubMed:3426581 ]
  8. Amuro N, Yamaura M, Goto Y, Okazaki T: Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor. Biochem Biophys Res Commun. 1988 May 16;152(3):1395-400. [PubMed:3377777 ]
  9. Nakatani Y, Schneider M, Banner C, Freese E: Complete nucleotide sequence of human glutamate dehydrogenase cDNA. Nucleic Acids Res. 1988 Jul 11;16(13):6237. [PubMed:3399399 ]
  10. Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N: Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc Natl Acad Sci U S A. 1988 May;85(10):3494-8. [PubMed:3368458 ]
  11. Michaelidis TM, Tzimagiorgis G, Moschonas NK, Papamatheakis J: The human glutamate dehydrogenase gene family: gene organization and structural characterization. Genomics. 1993 Apr;16(1):150-60. [PubMed:8486350 ]
  12. Julliard JH, Smith EL: Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J Biol Chem. 1979 May 10;254(9):3427-38. [PubMed:429360 ]
  13. Banner C, Silverman S, Thomas JW, Lampel KA, Vitkovic L, Huie D, Wenthold RJ: Isolation of a human brain cDNA for glutamate dehydrogenase. J Neurochem. 1987 Jul;49(1):246-52. [PubMed:3585334 ]
  14. Tzimagiorgis G, Leversha MA, Chroniary K, Goulielmos G, Sargent CA, Ferguson-Smith M, Moschonas NK: Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2. Hum Genet. 1993 Jun;91(5):433-8. [PubMed:8314555 ]
  15. Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA: Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J Mol Biol. 2001 Mar 23;307(2):707-20. [PubMed:11254391 ]
  16. Fang J, Hsu BY, MacMullen CM, Poncz M, Smith TJ, Stanley CA: Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J. 2002 Apr 1;363(Pt 1):81-7. [PubMed:11903050 ]
  17. Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA: The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol. 2002 May 3;318(3):765-77. [PubMed:12054821 ]
  18. Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ: Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry. 2003 Apr 1;42(12):3446-56. [PubMed:12653548 ]
  19. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed:10338089 ]
  20. Stanley CA, Lieu YK, Hsu BY, Burlina AB, Greenberg CR, Hopwood NJ, Perlman K, Rich BH, Zammarchi E, Poncz M: Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med. 1998 May 7;338(19):1352-7. [PubMed:9571255 ]
  21. Miki Y, Taki T, Ohura T, Kato H, Yanagisawa M, Hayashi Y: Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. J Pediatr. 2000 Jan;136(1):69-72. [PubMed:10636977 ]
  22. Santer R, Kinner M, Passarge M, Superti-Furga A, Mayatepek E, Meissner T, Schneppenheim R, Schaub J: Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. Hum Genet. 2001 Jan;108(1):66-71. [PubMed:11214910 ]
  23. MacMullen C, Fang J, Hsu BY, Kelly A, de Lonlay-Debeney P, Saudubray JM, Ganguly A, Smith TJ, Stanley CA: Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab. 2001 Apr;86(4):1782-7. [PubMed:11297618 ]