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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Glutamic-gamma-semialdehyde (HMDB02104)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:36
Update Date 2009-05-05 20:59:05
Accession Number HMDB02104
Secondary Accession Numbers Not Available
Common Name L-Glutamic-gamma-semialdehyde
Description Glutamic gamma-semialdehyde is the metabolic precursor for proline biosynthesis. The conversion from L-Glutamate, an ATP- and NADPH-dependent reaction, is catalyzed by the enzyme Delta-1-pyrroline-5-carboxylate synthetase (P5CS) (OMIM 138250). L-Glutamic-gamma-semialdehyde can also be converted to or be formed from the amino acids L-ornithine (EC 2.6.1.13) and L-proline (EC 1.5.99.8 and EC 1.5.1.2). It is also one of the few metabolites that can be a precursor to other metabolites of both the urea cycle and the citric acid cycle (BioCyc)
Synonyms
  1. L-glutamate gamma-semialdehyde
  2. L-glutamate-5-semialdehyde
  3. glutamate-semialdehyde
  4. glutamic gamma-semialdehyde
  5. L-Glutamic-gamma-semialdehyde
  6. L-glutamate 5-semialdehyde
Chemical IUPAC Name 2-amino-5-oxo-pentanoic acid
Chemical Formula C5H9NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • aldehyde
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 131.130
Monoisotopic Molecular Weight 131.058243
Isomeric SMILES N[C@@H](CCC=O)C(O)=O
Canonical SMILES NC(CCC=O)C(O)=O
KEGG Compound ID C01165 Link Image
BioCyc ID L-GLUTAMATE_GAMMA-SEMIALDEHYDE Link Image
BiGG ID 36962 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB02104 Link Image
Metagene Link HMDB02104 Link Image
METLIN ID 6488 Link Image
PubChem Compound 193305 Link Image
PubChem Substance 4392 Link Image
ChEBI ID 17232 Link Image
CAS Registry Number 496-92-4
InChI Identifier InChI=1/C5H9NO3/c6-4(5(8)9)2-1-3-7/h3-4H,1-2,6H2,(H,8,9)/t4-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 144.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.57 [Predicted by ALOGPS]; -2.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • mitochondria
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Arginine and Proline Metabolism SMP00020 Link Image map00330 Link Image
General References Not Available
Metabolic Enzymes
  1. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor
  2. Ornithine aminotransferase, mitochondrial precursor
  3. Delta 1-pyrroline-5-carboxylate synthetase
Enzyme 1 [top]
Enzyme 1 ID 5388
Enzyme 1 Name Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor
Enzyme 1 Synonyms
  1. P5C dehydrogenase
  2. Aldehyde dehydrogenase 4A1
Enzyme 1 Gene Name ALDH4A1
Enzyme 1 Protein Sequence >Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor 
MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGR
MEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKP
IADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVEL
EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAML
ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ
NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSL
WPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGK
CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTG
AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR
WTSPQVIKETHKPLGDWSYAYMQ
Enzyme 1 Number of Residues 563
Enzyme 1 Molecular Weight 61720
Enzyme 1 Theoretical pI 8.20
Enzyme 1 GO Classification
Function
  • 1-pyrroline-5-carboxylate dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • glutamine family amino acid metabolism
  • metabolism
  • physiological process
  • proline biosynthesis
  • proline metabolism
Component
  • membrane-enclosed lumen
  • mitochondrial lumen
  • mitochondrial matrix
  • organelle lumen
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes
Enzyme 1 Pathways
Enzyme 1 Reactions
  • 1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH + H+
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-19
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1353250 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P30038 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AL4A1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1692 bp 
ATGCTGCTGCCGGCGCCCGCGCTCCGCCGCGCCCTGCTGTCCCGCCCCTGGACCGGGGCC
GGCCTGCGGTGGAAGCACACCTCCTCCCTGAAGGTGGCCAACGAGCCCGTCTTAGCCTTC
ACGCAGGGCAGCCCTGAGCGAGATGCCCTGCAAAAGGCCTTGAAGGACCTGAAGGGCCGG
ATGGAAGCCATCCCATGCGTGATGGGGGATGAGGAGGTGTGGACGTCGGACGTGCAGTAC
CAAGTGTCGCCTTTTAACCATGGACATAAGGTGGCCAAGTTCTGTTATGCAGACAAGAGC
CTGCTCAACAAAGCCATTGAGGCTGCCCTGGCTGCCCGGAAAGAGTGGGACCTGAAGCCT
ATTGCAGACCGGGCCCAGATCTTCCTGAAGGCGGCAGACATGCTGAGTGGGCCGCGCAGG
GCTGAGATCCTCGCCAAGACCATGGTGGGACAGGGTAAGACCGTGATCCAAGCGGAGATT
GACGCTGCAGCGGAACTCATCGACTTCTTCCGGTTCAATGCCAAGTATGCGGTGGAGCTG
GAGGGGCAGCAGCCCATCAGCGTGCCCCCGAGCACCAACAGCACGGTGTACCGGGGTCTG
GAGGGCTTCGTGGCGGCCATCTCGCCCTTTAACTTCACTGCAATCGGCGGCAACCTGGCG
GGGGCACCGGCCCTGATGGGCAACGTGGTCCTATGGAAGCCCAGTGACACTGCCATGCTG
GCCAGCTATGCTGTCTACCGCATCCTTCGGGAGGCTGGCCTGCCCCCCAACATCATCCAG
TTTGTGCCAGCTGATGGGCCCCTATTTGGGGACACTGTCACCAGCTCAGAGCACCTCTGT
GGCATCAACTTCACAGGCAGTGTGCCCACCTTCAAACACCTGTGGAAGCAGGTGGCCCAG
AACCTGGACCGGTTCCACACCTTCCCACGCCTGGCTGGAGAGTGCGGCGGAAAGAACTTC
CACTTCGTGCACCGCTCGGCCGACGTGGAGAGCGTGGTGAGCGGGACCCTCCGCTCAGCC
TTCGAGTACGGTGGCCAGAAGTGTTCCGCCTGCTCGCGTCTCTACGTGCCGCACTCGCTG
TGGCCGCAGATCAAAGGGCGGCTGCTGGAGGAGCACAGTCGGATCAAAGTGGGCGACCCT
GCAGAGGATTTTGGGACCTTCTTCTCTGCAGTGATTGATGCCAAGTCCTTTGCCCGTATC
AAGAAGTGGCTGGAGCACGCGCGCTCCTCGCCCAGCCTCACCATCCTGGCTGGGGGCAAG
TGTGATGACTCCGTGGGCTACTTTGTGGAGCCCTGCATCGTGGAGAGCAAGGACCCTCAG
GAGCCCATCATGAAGGAGGAGATCTTCGGGCCTGTACTGTCTGTGTACGTCTACCCGGAC
GACAAGTACAAGGAGACGCTGCAGCTGGTTGACAGCACCACCAGCTATGGCCTCACGGGG
GCAGTGTTCTCCCAGGATAAGGACGTCGTGCAGGAGGCCACAAAGGTGCTGAGGAATGCT
GCCGGCAACTTCTACATCAACGACAAGTCCACTGGCTCGATAGTGGGCCAGCAGCCCTTT
GGGGGGGCCCGAGCCTCTGGAACCAATGACAAGCCAGGGGGCCCACACTACATCCTGCGC
TGGACGTCGCCGCAGGTCATCAAGGAGACACATAAGCCCCTGGGGGACTGGAGCTACGCG
TACATGCAGTGA
Enzyme 1 GenBank Gene ID U24267 Link Image
Enzyme 1 GeneCard ID ALDH4A1 Link Image
Enzyme 1 GenAtlas ID ALDH4A1 Link Image
Enzyme 1 HGNC ID HGNC:406 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p36
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Hu CA, Lin WW, Valle D: Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J Biol Chem. 1996 Apr 19;271(16):9795-800. [PubMed Link Image]
  2. Hempel J, Eckey R, Berie D, Romovacek H, Agarwal DP, Goedde HW: Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme. Comp Biochem Physiol B. 1992 Aug;102(4):791-93. [PubMed Link Image]
  3. 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 Link Image]
  4. Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA: Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum Mol Genet. 1998 Sep;7(9):1411-5. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5637
Enzyme 2 Name Ornithine aminotransferase, mitochondrial precursor
Enzyme 2 Synonyms
  1. Ornithine--oxo-acid aminotransferase[Contains: Ornithine aminotransferase, hepatic form
  2. Ornithine aminotransferase, renal form]
Enzyme 2 Gene Name OAT
Enzyme 2 Protein Sequence >Ornithine aminotransferase, mitochondrial precursor 
MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPV
ALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVL
GEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGR
TLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVV
PDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYP
VSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGIILRNEL
MKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCLRLRDNGLLAKPTHGDIIRFAPPLVI
KEDELRESIEIINKTILSF
Enzyme 2 Number of Residues 439
Enzyme 2 Molecular Weight 48535
Enzyme 2 Theoretical pI 7.05
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • pyridoxal phosphate binding
  • transaminase activity
  • transferase activity
  • transferase activity, transferring nitrogenous groups
  • vitamin binding
Process
—
Component
—
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function L-ornithine + a 2-oxo acid = L-glutamate 5- semialdehyde + an L-amino acid
Enzyme 2 Pathways
Enzyme 2 Reactions
  • L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-20
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 189329 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P04181 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name OAT_HUMAN Link Image
Enzyme 2 PDB ID 1OAT Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1320 bp 
ATGTTTTCCAAACTAGCACATTTGCAGAGGTTTGCTGTACTTAGTCGCGGAGTTCATTCT
TCAGTGGCTTCTGCTACATCTGTTGCAACTAAAAAAACAGTCCAAGGCCCTCCAACCTCT
GATGACATTTTTGAAAGGGAATATAAGTATGGTGCACACAACTACCATCCTTTACCTGTA
GCCCTGGAGAGAGGAAAAGGTATTTACTTATGGGATGTAGAAGGCAGAAAATATTTTGAC
TTCCTGAGTTCTTACAGTGCTGTCAACCAAGGGCATTGTCACCCCAAGATTGTGAATGCT
CTGAAGAGTCAAGTGGACAAATTGACCTTAACATCTAGAGCTTTCTATAATAACGTACTT
GGTGAATATGAGGAGTATATTACTAAACTTTTCAACTACCACAAAGTTCTTCCTATGAAT
ACAGGAGTGGAGGCTGGAGAGACTGCCTGTAAACTAGCTCGTAAGTGGGGCTATACCGTG
AAGGGCATTCAGAAATACAAAGCAAAGATTGTTTTTGCAGCTGGGAACTTCTGGGGTAGG
ACGTTGTCTGCTATCTCCAGTTCCACAGACCCAACCAGTTACGATGGTTTTGGACCATTT
ATGCCGGGATTCGACATCATTCCCTATAATGATCTGCCCGCACTGGAGCGTGCTCTTCAG
GATCCAAATGTGGCTGCGTTCATGGTAGAACCAATTCAGGGTGAAGCAGGCGTTGTTGTT
CCGGATCCAGGTTACCTAATGGGAGTGCGAGAGCTCTGCACCAGGCACCAGGTTCTCTTT
ATTGCTGATGAAATACAGACAGGATTGGCCAGAACTGGTAGATGGCTGGCTGTTGATTAT
GAAAATGTCAGACCTGATATAGTCCTCCTTGGAAAGGCCCTTTCTGGGGGCTTATACCCT
GTGTCTGCAGTGCTGTGTGATGATGACATCATGCTGACCATTAAGCCAGGGGAGCATGGG
TCCACATACGGTGGCAATCCACTAGGCTGCCGAGTGGCCATCGCAGCCCTTGAGGTTTTA
GAAGAAGAAAACCTTGCTGAAAATGCAGACAAATTGGGCATTATCTTGAGAAATGAACTC
ATGAAGCTACCTTCTGATGTTGTAACTGCCGTAAGAGGAAAAGGATTATTAAACGCTATT
GTCATTAAAGAAACCAAAGATTGGGATGCTTGGAAGGTGTGTCTACGACTTCGAGATAAT
GGACTTCTGGCCAAGCCAACCCATGGCGACATTATCAGGTTTGCGCCTCCGCTGGTGATC
AAGGAGGATGAGCTTCGAGAGTCCATTGAAATTATTAACAAGACCATCTTGTCTTTCTGA
Enzyme 2 GenBank Gene ID M12267 Link Image
Enzyme 2 GeneCard ID OAT Link Image
Enzyme 2 GenAtlas ID OAT Link Image
Enzyme 2 HGNC ID HGNC:8091 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Inana G, Totsuka S, Redmond M, Dougherty T, Nagle J, Shiono T, Ohura T, Kominami E, Katunuma N: Molecular cloning of human ornithine aminotransferase mRNA. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1203-7. [PubMed Link Image]
  2. Ramesh V, Shaffer MM, Allaire JM, Shih VE, Gusella JF: Investigation of gyrate atrophy using a cDNA clone for human ornithine aminotransferase. DNA. 1986 Dec;5(6):493-501. [PubMed Link Image]
  3. Kobayashi T, Nishii M, Takagi Y, Titani K, Matsuzawa T: Molecular cloning and nucleotide sequence analysis of mRNA for human kidney ornithine aminotransferase. An examination of ornithine aminotransferase isozymes between liver and kidney. FEBS Lett. 1989 Sep 25;255(2):300-4. [PubMed Link Image]
  4. Mitchell GA, Looney JE, Brody LC, Steel G, Suchanek M, Engelhardt JF, Willard HF, Valle D: Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the structural gene. J Biol Chem. 1988 Oct 5;263(28):14288-95. [PubMed Link Image]
  5. Zintz CB, Inana G: Analysis of the human ornithine aminotransferase gene family. Exp Eye Res. 1990 Jun;50(6):759-70. [PubMed Link Image]
  6. Ramesh V, Gusella JF, Shih VE: Molecular pathology of gyrate atrophy of the choroid and retina due to ornithine aminotransferase deficiency. Mol Biol Med. 1991 Feb;8(1):81-93. [PubMed Link Image]
  7. Simmaco M, John RA, Barra D, Bossa F: The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis. FEBS Lett. 1986 Apr 7;199(1):39-42. [PubMed Link Image]
  8. Shah SA, Shen BW, Brunger AT: Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition. Structure. 1997 Aug 15;5(8):1067-75. [PubMed Link Image]
  9. Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T: Crystal structure of human recombinant ornithine aminotransferase. J Mol Biol. 1998 Mar 20;277(1):81-102. [PubMed Link Image]
  10. Storici P, Capitani G, Muller R, Schirmer T, Jansonius JN: Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine. J Mol Biol. 1999 Jan 8;285(1):297-309. [PubMed Link Image]
  11. Ramesh V, McClatchey AI, Ramesh N, Benoit LA, Berson EL, Shih VE, Gusella JF: Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy. Proc Natl Acad Sci U S A. 1988 Jun;85(11):3777-80. [PubMed Link Image]
  12. Inana G, Chambers C, Hotta Y, Inouye L, Filpula D, Pulford S, Shiono T: Point mutation affecting processing of the ornithine aminotransferase precursor protein in gyrate atrophy. J Biol Chem. 1989 Oct 15;264(29):17432-6. [PubMed Link Image]
  13. Michaud J, Brody LC, Steel G, Fontaine G, Martin LS, Valle D, Mitchell G: Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene. Genomics. 1992 Jun;13(2):389-94. [PubMed Link Image]
  14. Brody LC, Mitchell GA, Obie C, Michaud J, Steel G, Fontaine G, Robert MF, Sipila I, Kaiser-Kupfer M, Valle D: Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences. J Biol Chem. 1992 Feb 15;267(5):3302-7. [PubMed Link Image]
  15. Michaud J, Thompson GN, Brody LC, Steel G, Obie C, Fontaine G, Schappert K, Keith CG, Valle D, Mitchell GA: Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V. Am J Hum Genet. 1995 Mar;56(3):616-22. [PubMed Link Image]
  16. Kobayashi T, Ogawa H, Kasahara M, Shiozawa Z, Matsuzawa T: A single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursor. Am J Hum Genet. 1995 Aug;57(2):284-91. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6135
Enzyme 3 Name Delta 1-pyrroline-5-carboxylate synthetase
Enzyme 3 Synonyms
  1. P5CS
  2. Aldehyde dehydrogenase 18 family member A1[Includes: Glutamate 5-kinase
  3. Gamma-glutamyl kinase
  4. GK
  5. Gamma-glutamyl phosphate reductase
  6. GPR
  7. Glutamate-5-semialdehyde dehydrogenase
  8. Glutamyl-gamma-semialdehyde dehydrogenase]
Enzyme 3 Gene Name ALDH18A1
Enzyme 3 Protein Sequence >Delta 1-pyrroline-5-carboxylate synthetase 
MLSQVYRCGFQPFNQHLLPWVKCTTVFRSHCIQPSVIRHVRSWSNIPFITVPLSRTHGKS
FAHRSELKHAKRIVVKLGSAVVTRGDECGLALGRLASIVEQVSVLQNQGREMMLVTSGAV
AFGKQRLRHEILLSQSVRQALHSGQNQLKEMAIPVLEARACAAAGQSGLMALYEAMFTQY
SICAAQILVTNLDFHDEQKRRNLNGTLHELLRMNIVPIVNTNDAVVPPAEPNSDLQGVNV
ISVKDNDSLAARLAVEMKTDLLIVLSDVEGLFDSPPGSDDAKLIDIFYPGDQQSVTFGTK
SRVGMGGMEAKVKAALWALQGGTSVVIANGTHPKVSGHVITDIVEGKKVGTFFSEVKPAG
PTVEQQGEMARSGGRMLATLEPEQRAEIIHHLADLLTDQRDEILLANKKDLEEAEGRLAA
PLLKRLSLSTSKLNSLAIGLRQIAASSQDSVGRVLRRTRIAKNLELEQVTVPIGVLLVIF
ESRPDCLPQVAALAIASGNGLLLKGGKEAAHSNRILHLLTQEALSIHGVKEAVQLVNTRE
EVEDLCRLDKMIDLIIPRGSSQLVRDIQKAAKGIPVMGHSEGICHMYVDSEASVDKVTRL
VRDSKCEYPAACNALETLLIHRDLLRTPLFDQIIDMLRVEQVKIHAGPKFASYLTFSPSE
VKSLRTEYGDLELCIEVVDNVQDAIDHIHKYGSSHTDVIVTEDENTAEFFLQHVDSACVF
WNASTRFSDGYRFGLGAEVGISTSRIHARGPVGLEGLLTTKWLLRGKDHVVSDFSEHGSL
KYLHENLPIPQRNTN
Enzyme 3 Number of Residues 795
Enzyme 3 Molecular Weight 87304
Enzyme 3 Theoretical pI 7.13
Enzyme 3 GO Classification
Function
  • catalytic activity
  • glutamate 5-kinase activity
  • glutamate-5-semialdehyde dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • amino acid and derivative metabolism
  • amino acid biosynthesis
  • amino acid metabolism
  • cellular metabolism
  • glutamine family amino acid metabolism
  • metabolism
  • physiological process
  • proline biosynthesis
  • proline metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function ATP + L-glutamate = ADP + L-glutamate 5- phosphate
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • ATP + L-glutamate = ADP + L-glutamate 5-phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1304314 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P54886 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name P5CS_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >2388 bp 
ATGTTGAGTCAAGTTTACCGCTGTGGGTTCCAGCCCTTCAACCAACATCTTCTGCCCTGG
GTCAAGTGTACAACCGTCTTCAGATCTCATTGTATCCAGCCTTCAGTCATCAGACATGTT
CGTTCTTGGAGCAACATCCCGTTTATCACTGTACCCCTCAGTCGTACACATGGCAAGTCC
TTCGCCCACCGCAGTGAGCTGAAGCATGCCAAGAGAATCGTGGTGAAGCTCGGCAGTGCC
GTGGTGACCCGAGGGGATGAATGTGGCCTGGCCCTGGGGCGCTTGGCATCTATTGTTGAG
CAGGTATCAGTGCTGCAGAATCAGGGCAGAGAGATGATGCTGGTGACCAGTGGAGCCGTA
GCCTTTGGCAAACAAACGTTGCGCCATGAGATCCTTCTGTCTCAGAGCGTGCGGCAGGCC
CTCCACTCGGGGCAGAACCAGCTGAAAGAAATGGCAATTCCAGTCTTAGAGGCACGAGCC
TGTGCAGCTGCCGGACAGAGTGGGCTGATGGCCTTGTATGAGGCTATGTTTACCCAGTAC
AGCATCTGTGCTGCCCAGATTTTGGTGACCAATTTGGATTTCCATGATGAGCAGAAGCGC
CGGAACCTCAATGGAACACTTCATGAACTCCTTAGAATGAACATTGTCCCCATTGTCAAC
ACAAATGATGCTGTTGTCCCCCCAGCTGAGCCCAACAGTGACCTGCAGGGGGTAAATGTT
ATTAGTGTTAAAGATAATGATAGCCTGGCTGCCCGACTGGCTGTGGAAATGAAAACTGAT
CTCTTGATTGTCCTTCCAGATGTAGAAGGCCTTTTTGACAGCCCCCCAGGTTCAGATGAT
GCAAAGCTTATTGATATATTTTATCCCGGAGATCAGCAGTCTGTGACATTTGGACCCAAG
TCTAGAGTGGGAAATGGGTGCATGGAAGCCAAGGTGAAAAGCACCCTCTGGGCTTTGCAA
GGTGGCACTTCTGTTGTTATTGCCAATGGAACCCACCCAAAGGTGTCTGGGCACGTCATC
ACAGACATTGTGGAGGGGAAGAAAGTTGGTACCTTCTTTTCAGAAGTAAAGCCTGCAGGC
CCTACTGTTGAGCAGCAGGGAGAAATGGCGCGATCTGGAGGAAGGATGTTGGCCACCTTG
GAACCTGAGCAGAGAGCAGAAATTATCCATCATCTGGCTGATCTGTTGACGGACCAGCGT
GATGAGATCCTGTTAGCCAACAAAAAAGACTTGGAGGAGGCAGAGGGGAGACTTGCAGCT
CCTCTGCTGAAACGTTTAAGCCTCTCCACATCCAAATTGAACAGCCTGGCCATCGGTCTG
CGACAGATCGCAGCCTCCTCCCAGGACAGCGTGGGACGTGTTTTGCGCCGCACCCGAATC
GCCAAAAACTTGGAACTGGAACAAGTGACTGTCCCAATTGGAGTTCTGCTGGTGATCTTT
GAATCTCGTCCTGACTGTCCTACCCCAGGTGGCAGCTTTGCTATCGCAAGTGGCAATGGC
TTGTTACTCAAAGGAGGGAAGGAGGCTGCACACAGCAACCGGATTCTCCACCTCCTGACC
CAGGAGGCTCTCTCAATCCATGGAGTCAAGGAGGCCGTGCAACTGGTGAATACCAGAGAA
GAAGTTGAAGATCTTTGCCGCCTAGACAAAATGATAGATCTGATCATTCCACGTGGCTCT
TCCCAGCTGGTCAGAGACATCCAGAAAGCTGCTAAGGGGATTCCAGTGATGGGGCACAGC
GAAGGGATCTGTCACATGTATGTGGATTCCGAGGCCAGTGTTGATAAGGTCACCAGGCTA
GTCAGAGACTCTAAATGTGAATATCCAGCTGCCTGTAATGCTTTGGAGACTTTGTTAATC
CACCGGGATCTGCTCAGGACACCATTATTTGACCAGATCATTGATATGCTGAGAGTGGAA
CAGGTAAAAATTCATGCAGGCCCCAAATTTGCCTCCTATCTGACCTTCAGCCCCTCCGAA
GTGAAGTCACTCCGAACTGAGTATGGGGACCTGGAATTATGCATTGAAGTAGTGGACAAC
GTTCAGGATGCCATTGACCACATCCACAAGTATGGCAGCTCCCACACGGATGTCATCGTC
ACAGAGGACGAAAACACAGCGGAGTTCTTCCTGCAGCACGTAGACAGTGCCTGTGTGTTC
TGGAATGCCAGCACTCGCTTTTCTGATGGTTACCGCTTTGGACTGGGAGCTGAAGTGGGA
ATCAGTACATCGAGAATCCACGCCCGGGGACCAGTAGGACTTGAGGGACTGCTTACTACT
AAGTGGCTGCTGCGAGGGAAGGACCACGTGGTCTCAGATTTCTCAGAGCATGGAAGTTTA
AAATATCTTCATGAGAACCTCCCTATTCCTCAGAGAAACACCAACTGA
Enzyme 3 GenBank Gene ID X94453 Link Image
Enzyme 3 GeneCard ID ALDH18A1 Link Image
Enzyme 3 GenAtlas ID ALDH18A1 Link Image
Enzyme 3 HGNC ID HGNC:9722 Link Image
Enzyme 3 Chromosome Location 10
Enzyme 3 Locus 10q24.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Aral B, Schlenzig JS, Liu G, Kamoun P: Database cloning human delta 1-pyrroline-5-carboxylate synthetase (P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in proline biosynthesis. C R Acad Sci III. 1996 Mar;319(3):171-8. [PubMed Link Image]
  2. Hu CA, Lin WW, Obie C, Valle D: Molecular enzymology of mammalian Delta1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem. 1999 Mar 5;274(10):6754-62. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available