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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Threonine (HMDB00167)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-08 15:15:00
Accession Number HMDB00167
Secondary Accession Numbers Not Available
Common Name L-Threonine
Description Threonine is an essential amino acid in humans. It is abundant in human plasma, particularly in newborns. Severe deficiency of threonine causes neurological dysfunction and lameness in experimental animals. Threonine is an immunostimulant which promotes the growth of thymus gland. It also can probably promote cell immune defense function. This amino acid has been useful in the treatment of genetic spasticity disorders and multiple sclerosis at a dose of 1 gram daily. It is highly concentrated in meat products, cottage cheese and wheat germ. (http://www.dcnutrition.com/AminoAcids/) The threonine content of most of the infant formulas currently on the market is approximately 20% higher than the threonine concentration in human milk. Due to this high threonine content the plasma threonine concentrations are up to twice as high in premature infants fed these formulas than in infants fed human milk. The whey proteins which are used for infant formulas are sweet whey proteins. Sweet whey results from cheese production. Threonine catabolism in mammals appears to be due primarily (70-80%) to the activity of threonine dehydrogenase (EC 1.1.1.103) that oxidizes threonine to 2-amino-3-oxobutyrate, which forms glycine and acetyl CoA, whereas threonine dehydratase (EC 4.2.1.16) that catabolizes threonine into 2-oxobutyrate and ammonia, is significantly less active. Increasing the threonine plasma concentrations leads to accumulation of threonine and glycine in the brain. Such accumulation affects the neurotransmitter balance which may have consequences for the brain development during early postnatal life. Thus, excessive threonine intake during infant feeding should be avoided. (PMID 9853925)
Synonyms
  1. (2S,3R)-(-)-Threonine
  2. (2S,3R)-2-Amino-3-hydroxybutyrate
  3. (2S,3R)-2-Amino-3-hydroxybutyric acid
  4. (R-(R*,S*))-2-Amino-3-hydroxybutanoate
  5. (R-(R*,S*))-2-Amino-3-hydroxybutanoic acid
  6. (S)-Threonine
  7. 2-Amino-3-hydroxybutanoate
  8. 2-Amino-3-hydroxybutanoic acid
  9. 2-Amino-3-hydroxybutyrate
  10. 2-Amino-3-hydroxybutyric acid
  11. L-(-)-Threonine
  12. L-2-Amino-3-hydroxybutyrate
  13. L-2-Amino-3-hydroxybutyric acid
  14. L-alpha-Amino-beta-hydroxybutyrate
  15. L-alpha-Amino-beta-hydroxybutyric acid
  16. Threonin
  17. Threonine
  18. [R-(R*,S*)]-2-Amino-3-hydroxybutanoate
  19. [R-(R*,S*)]-2-Amino-3-hydroxybutanoic acid
  20. [R-(R*,S*)]-2-amino-3-hydroxy-Butanoate
  21. [R-(R*,S*)]-2-amino-3-hydroxy-Butanoic acid
Chemical IUPAC Name 2-amino-3-hydroxy-butanoic acid
Chemical Formula C4H9NO3
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
  • secondary alcohol
  • 1,2-aminoalcohol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Essential amino acids
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Glycine, serine and threonine metabolism
Application
—
Source
  • Exogenous
Average Molecular Weight 119.119
Monoisotopic Molecular Weight 119.058243
Isomeric SMILES C[C@@H](O)[C@H](N)C(O)=O
Canonical SMILES CC(O)C(N)C(O)=O
KEGG Compound ID C00188 Link Image
BioCyc ID THR Link Image
BiGG ID 34186 Link Image
Wikipedia Link L-Threonine Link Image
NuGOwiki Link HMDB00167 Link Image
Metagene Link HMDB00167 Link Image
METLIN ID 32 Link Image
PubChem Compound 6288 Link Image
PubChem Substance 841559 Link Image
ChEBI ID 16857 Link Image
CAS Registry Number 72-19-5
InChI Identifier InChI=1/C4H9NO3/c1-2(6)3(5)4(7)8/h2-3,6H,5H2,1H3,(H,7,8)/t2-,3+/m1/s1
Synthesis Reference Fujita, Chuzo; Nara, Takashi; Samejima, Hirotoshi; Kinoshita, Shukuo. L-Threonine fermentation. I. Microbial conversion of L-homoserine to L-threonine. Nippon Nogei Kagaku Kaishi (1965), 39(6), 2
Melting Point (Experimental) 256 oC
Experimental Water Solubility 97.0 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 477.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -2.94 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity -3.01 [Predicted by ALOGPS]; -3.5 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1EVK Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Blood
Value 140.0 (107.0-173.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
Biofluid Blood
Value 215.0 +/- 60.0 uM
Age Newborn:0-30 days old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 140.0 +/- 28.0 uM
Age Children:1-13 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 146.0 +/- 22.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 154.0 +/- 40.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 92. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Blood
Value 260.0 +/- 10.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid CSF
Value 27.7 +/- 4.7 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 32.0 (4.00-60.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51. [PubMed Link Image]
Biofluid CSF
Value 45.9 +/- 12.3 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 37.4 +/- 7.6 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 34.7 +/- 6.2 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
Biofluid CSF
Value 30 +/- 12 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid CSF
Value 10.35 +/- 0.88 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid Saliva
Value >10 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
Biofluid Urine
Value 36.20 +/- 25.38 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Biofluid Urine
Value 12.7 (4.934-20.4) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 1.0 (0.16-2.4) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 4.9 +/- 2.5 umol/mmol creatinine
Age Children:1-13 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 18.0 +/- 9.6 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 16.0 +/- 9.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 10.3 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guo K, Li L: Differential (12)C-/(13)C-Isotope Dansylation Labeling and Fast Liquid Chromatography/Mass Spectrometry for Absolute and Relative Quantification of the Metabolome. Anal Chem. 2009 Mar 23. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 114.0 +/- 9.2 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Acute seizures
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 118.0 +/- 3.8 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Refractory localization-related epilepsy (RLE)
References
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Biofluid Blood
Value 227.0 +/- 10.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Heart failure
Comments Non-diabetic patients with chronic heart failure
References
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Biofluid CSF
Value 41.0 +/- 15.9 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Not Available
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 30.2 +/- 9.8 uM
Age Children:1-13 yrs old
Sex N/A
Condition Leukemia
Comments Acute Lymphoblastic Leukemia (ALL) with Central Nervous System (CNS) disease
References
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Biofluid CSF
Value 9.68 +/- 2.22 uM
Age Adult:>18 yrs old
Sex Both
Condition Schizophrenia
Comments Not Available
References
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
Biofluid Urine
Value 0.03 +/- 0.003 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Associated Disorders
Condition References
Alzheimer's disease
  • Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. [PubMed Link Image]
Epilepsy
  • Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
Heart failure
  • Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. [PubMed Link Image]
Leukemia
  • Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
Schizophrenia
  • Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Threonine and 2-Oxobutanoate Degradation SMP00452 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Vold BS, Keith DE Jr, Slavik M: Urine levels of N-[9-(beta-D-ribofuranosyl)purin-6-ylcarbamoyl]-L-threonine, N6-(delta 2-isopentenyl)adenosine, and 2'-O-methylguanosine as determined by radioimmunoassay for normal subjects and cancer patients. Cancer Res. 1982 Dec;42(12):5265-9. [PubMed Link Image]
  2. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. [PubMed Link Image]
  3. Hallgren P, Lundblad A, Svensson S: A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine. J Biol Chem. 1975 Jul 25;250(14):5312-4. [PubMed Link Image]
  4. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. [PubMed Link Image]
  5. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. [PubMed Link Image]
  6. Wevers RA, Engelke U, Wendel U, de Jong JG, Gabreels FJ, Heerschap A: Standardized method for high-resolution 1H-NMR of cerebrospinal fluid. Clin Chem. 1995 May;41(5):744-51. [PubMed Link Image]
  7. Wulf G, Finn G, Suizu F, Lu KP: Phosphorylation-specific prolyl isomerization: is there an underlying theme? Nat Cell Biol. 2005 May;7(5):435-41. [PubMed Link Image]
  8. Takeda DY, Parvin JD, Dutta A: Degradation of Cdt1 during S phase is Skp2-independent and is required for efficient progression of mammalian cells through S phase. J Biol Chem. 2005 Jun 17;280(24):23416-23. Epub 2005 Apr 25. [PubMed Link Image]
  9. Nanda N, Bao M, Lin H, Clauser K, Komuves L, Quertermous T, Conley PB, Phillips DR, Hart MJ: Platelet endothelial aggregation receptor 1 (PEAR1), a novel epidermal growth factor repeat-containing transmembrane receptor, participates in platelet contact-induced activation. J Biol Chem. 2005 Jul 1;280(26):24680-9. Epub 2005 Apr 25. [PubMed Link Image]
  10. Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. [PubMed Link Image]
  11. Boneh A, Korman SH, Sato K, Kanno J, Matsubara Y, Lerer I, Ben-Neriah Z, Kure S: A single nucleotide substitution that abolishes the initiator methionine codon of the GLDC gene is prevalent among patients with glycine encephalopathy in Jerusalem. J Hum Genet. 2005;50(5):230-4. Epub 2005 Apr 29. [PubMed Link Image]
  12. Elzinga M, Maron BJ, Adelstein RS: Human heart and platelet actins are products of different genes. Science. 1976 Jan 9;191(4222):94-5. [PubMed Link Image]
  13. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. [PubMed Link Image]
  14. Rodriguez-Soriano J, Vallo A, Perez de Nanclares G, Bilbao JR, Castano L: A founder mutation in the CLCNKB gene causes Bartter syndrome type III in Spain. Pediatr Nephrol. 2005 Jul;20(7):891-6. Epub 2005 May 5. [PubMed Link Image]
  15. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. [PubMed Link Image]
  16. Wikipedia Link Image
Metabolic Enzymes
  1. Threonyl-tRNA synthetase, cytoplasmic
  2. Neutral amino acid transporter A
  3. Threonine synthase-like 1
  4. ILVBL protein
  5. cDNA FLJ75173, highly similar to Homo sapiens threonyl-tRNA synthetase, mRNA
  6. Probable threonyl-tRNA synthetase 2, cytoplasmic
  7. Threonyl-tRNA synthetase, mitochondrial
Enzyme 1 [top]
Enzyme 1 ID 5853
Enzyme 1 Name Threonyl-tRNA synthetase, cytoplasmic
Enzyme 1 Synonyms
  1. Threonine--tRNA ligase
  2. ThrRS
Enzyme 1 Gene Name TARS
Enzyme 1 Protein Sequence >Threonyl-tRNA synthetase, cytoplasmic 
MFEEKASSPSGKMGGEEKPIGAGEEKQKEGGKKKNKEGSGDGGRAELNPWPEYIYTRLEM
YNILKAEHDSILAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIA
KVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIE
NGFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRIL
NEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGI
SFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFI
RSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMF
DHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL
DFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFY
GPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERM
IAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNK
KIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAE
EEF
Enzyme 1 Number of Residues 723
Enzyme 1 Molecular Weight 83436
Enzyme 1 Theoretical pI 6.64
Enzyme 1 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
  • threonine-tRNA ligase activity
  • transition metal ion binding
  • transporter activity
Process
  • RNA metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • protein biosynthesis
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
  • threonyl-tRNA aminoacylation
Component
—
Enzyme 1 General Function Translation, ribosomal structure and biogenesis
Enzyme 1 Specific Function ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Enzyme 1 Pathways
  • Aminoacyl-tRNA biosynthesis (map00970 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 1 Reactions
  • ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1464742 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P26639 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SYTC_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2139 bp 
ATGGGAGGCGAGGAGAAGCCGATTGGTGCTGGTGAAGAGAAGCAAAAGGAAGGAGGCAAA
AAGAAGAACAAAGAAGGATCTGGAGATGGAGGTCGAGCTGAGTTGAATCCTTGGCCTGAA
TATATTTACACACGTCTTGAGATGTATAATATACTAAAAGCAGAACATGATTCCATTCTG
GCAGAAAAGGCAGAAAAAGATAGCAAGCCAATTAAAGTCACTTTGCCTGATGGTAAACAG
GTTGATGCGGAATCTTGGAAAACTACACCATATCAAATTGCCTGTGGAATTAGTCAAGGC
CTGGCCGACAACACCGTTATTGCTAAAGTAAATAATGTTGTGTGGGACCTGGACCGCCCT
CTGGAAGAAGATTGTACCTTGGAGCTTCTCAAGTTTGAGGATGAGGAAGCTCAGGCAGTG
TATTGGCACTCTAGTGCTCACATAATGGGTGAAGGCATGGAAAGAGTCTATGGTGGATGT
TTATGCTACGGTCCGCCAATAGAAAATGGATTCTATTATGACATGTACCTCGAAGAAGGG
GGTGTGTCTAGCAATGATTTCTCTTCTCTGGAGGCTTTGTGTAAGAAAATCATTAAAGAA
AAACAAGCTTTTGAAAGACTGGAAGTTAAGAAAGAAACTTTACTGGCAATGTTTAAGTAC
AACAAGTTCAAATGCCGGATATTGAATGAAAAGGTGAATACTCCAACTACCACAGTCTAT
AGATGTGGCCCTTTGATAGATCTCTGCCGGGGTCCTCATGTTAGACACACGGGCAAAATT
AAGGCTTTAAAAATACACAAAAATTCCTCCACGTACTGGGAAGGCAAAGCAGATATGGAG
ACTCTCCAGAGAATTTATGGCATTTCATTCCCAGATCCTAAAATGTTGAAAGAGTGGGAG
AAGTTCCAAGAGGAAGCTAAAAACCGAGATCATAGGAAAATTGGCAGGGACCAAGAACTA
TATTTCTTTCATGAACTCAGCCCTGGAAGTTGCTTTTTTCTGCCAAAAGGAGTCTATATT
TATAATGCACTTATTGAATTCATTAGGAGCGAATATAGGAAAAGAGGATTCCAGGAGGTA
GTCACCCCAAACATCTTCAACAGCCGACTCTGGATGACCTCGGGCCACTGGCAGCACTAC
AGCGAGAACATGTTCTCCTTTGAGGTGGAGAAGGAGCTGTTTGCCCTGAAACCCATGAAC
TGCCCAGGACACTCCCTTATGTTTGATCATCGGCCAAGGTCCTGGCGAGAACTGCCTCTG
CGGCTAGCTGATTTTGGGGGTCTTCATAGGAACGAGCTGTCTGGAGCACTCACAGGACTC
ACCCGGGTACGAAGATTCCAACAGGATGATGCTCACATATTCTGTGCCATGGAGCAGATT
GAAGATGAAATAAAAGGTTGTTTGGATTTTCTACGTACGGTATATAGCGTATTTGGATTT
TCTTTTAAACTAAACCTTTCTACTCGCCCGGAAAAATTCCTTGGAGATATCGAAGTATGG
GATCAAGCTGAGAAACAACTTGAAAACAGTCTGAATGAATTTGGTGAAAAGTGGGAGTTA
AACTCTGGAGATGGAGCTTTCTATGGCCCAAAGATTGACATACAGATTAAAGATGCGATT
GGGCGGTACCACCAGTGTGCAACCATCCAGCTGGATTTCCAGTTGCCCATCAGATTTAAT
CTTACTTATGTAAGCCATGATGGTGAGGATAAGAAAAGGCCAGTGATTGTTCATCGAGCC
ATCTTGGGATCAGTGGAAAGAATGATTGCTATCCTCACAGAAAACTATGGGGGCAAATTG
GCCCCCTTTTGGCTGTCCCCTCGCCAGGTAATGGTAGTTCCAGTGGGACCAACCTGTGAT
GAATATGCCCAAAACGTACGACAACAATTCCACGATGCCAAATTCATGGCAGACATTGAT
CTGGATCCAGGCTGTACATTGAATAAAAAGATTCGAAATGCACAGTTAGCACAGTATAAC
TTCATTTTAGTTGTTGGTGAAAAAGAGAAAATCACTGGCACTGTTAATATCCGCACAAGA
GACAATAAGGTCCACGGGGAACGCACCATTTCTGAAACTATCGAGCGGCTACAGCAGCTC
AAAGAGTTCCGCAGCAAACAGGCAGAAGAAGAATTTTAA
Enzyme 1 GenBank Gene ID M63180 Link Image
Enzyme 1 GeneCard ID TARS Link Image
Enzyme 1 GenAtlas ID TARS Link Image
Enzyme 1 HGNC ID HGNC:11572 Link Image
Enzyme 1 Chromosome Location 5
Enzyme 1 Locus 5p13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Cruzen ME, Arfin SM: Nucleotide and deduced amino acid sequence of human threonyl-tRNA synthetase reveals extensive homology to the Escherichia coli and yeast enzymes. J Biol Chem. 1991 May 25;266(15):9919-23. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 8650
Enzyme 2 Name Neutral amino acid transporter A
Enzyme 2 Synonyms
  1. SATT
  2. Solute carrier family 1 member 4
  3. Alanine/serine/cysteine/ threonine transporter
  4. ASCT1
Enzyme 2 Gene Name SLC1A4
Enzyme 2 Protein Sequence >Neutral amino acid transporter A 
MEKSNETNGYLDSAQAGPAAGPGAPGTAAGRARRCAGFLRRQALVLLTVSGVLAGAGLGA
ALRGLSLSRTQVTYLAFPGEMLLRMLRMIILPLVVCSLVSGAASLDASCLGRLGGIAVAY
FGLTTLSASALAVALAFIIKPGSGAQTLQSSDLGLEDSGPPPVPKETVDSFLDLARNLFP
SNLVVAAFRTYATDYKVVTQNSSSGNVTHEKIPIGTEIEGMNILGLVLFALVLGVALKKL
GSEGEDLIRFFNSLNEATMVLVSWIMWYVPVGIMFLVGSKIVEMKDIIVLVTSLGKYIFA
SILGHVIHGGIVLPLIYFVFTRKNPFRFLLGLLAPFATAFATCSSSATLPSMMKCIEENN
GVDKRISRFILPIGATVNMDGAAIFQCVAAVFIAQLNNVELNAGQIFTILVTATASSVGA
AGVPAGGVLTIAIILEAIGLPTHDLPLILAVDWIVDRTTTVVNVEGDALGAGILHHLNQK
ATKKGEQELAEVKVEAIPNCKSEEETSPLVTHQNPAGPVASAPELESKESVL
Enzyme 2 Number of Residues 532
Enzyme 2 Molecular Weight 55724
Enzyme 2 Theoretical pI 6.18
Enzyme 2 GO Classification
Function
  • carboxylic acid transporter activity
  • dicarboxylic acid transporter activity
  • organic acid transporter activity
  • sodium:dicarboxylate symporter activity
  • transporter activity
Process
  • carboxylic acid transport
  • cellular physiological process
  • dicarboxylic acid transport
  • organic acid transport
  • physiological process
  • transport
Component
  • cell
  • membrane
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-104
Enzyme 2 Transmembrane Regions
  • 42-62 88-108 119-139 217-237 257-277 298-318 328-348 373-393 418-438
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 348012 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P43007 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name SATT_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1599 bp 
ATGGAGAAGAGCAACGAGACCAACGGCTACCTTGACAGCGCTCAGGCGGGGCCTGCGGCC
GGGCCCGGAGCTCCGGGGACCGCGGCGGGACGCGCACGGCGTTGCGCGCGCTTCCTGCGG
CGCCAAGCGCTGGTGCTGCTCACCGTGTCCGGGGTGCTGGCGGGCGCGGGCCTGGGCGCG
GCGTTGCGCGGGCTCAGCCTGAGCCGCACGCAGGTCACCTACCTGGCCTTCCCCGGCGAG
ATGCTGCTCCGCATGCTGCGCATGATCATCCTGCCGCTGGTGGTCTGCAGCCTGGTGTCG
GGCGCCGCCTCGCTCGATGCCAGCTGCCTCGGGCGTCTGGGCGGCATCCGTGTCGCCTAC
TTTGGCCTCACCACACTGAGTGCCTCGGCGCTCGCCGTGGCCTTGGCGTTCATCATCAAG
CCAGGATCCGGTGCGCAGACCCTTCAGTCCAGCGACCTGGGGCTGGAGGACTCGGGGCCT
CCTCCTGTCCCCAAAGAGACGGTGGACTCTTTCCTCGACCTGGCCAGAAACCTGTTTCCC
TCCAATCTTGTGGTTGCAGCTTTCCGTACGTATGCAACCGATTATAAAGTCGTGACCCAG
AACAGCAGCTCTGGAAATGTAACCCATGAAAAGATCCCCATAGGCACTGAGATAGAAGGG
ATGAACATTTTAGGATTGGTCCTGTTTGCTCTGGTGTTAGGAGTGGCCTTAAAGAAACTA
GGCTCCGAAGGAGAAGACCTCATCCGTTTCTTCAATTCCCTCAACGAGGCGACGATGGTG
CTGGTGTCCTGGATTATGTGGTACGTACCTGTGGGCATCATGTTCCTTGTTGGAAGCAAG
ATCGTGGAAATGAAAGACATCATCGTGCTGGTGACCAGCCTGGGGAAATACATCTTCGCA
TCTATATTGGGCCATGTTATTCATGGAGGAATTGTTCTGCCACTTATTTATTTTGTTTTC
ACACGAAAAAACCCATTCAGATTCCTCCTGGGCCTCCTCGCCCCATTTGCGACAGCATTT
GCTACCTGCTCCAGCTCAGCGACCCTTCCCTCTATGATGAAGTGCATTGAAGAGAACAAT
GGTGTGGACAAGAGGATCAGCAGGTTTATTCTCCCCATCGGGGCCACCGTGAACATGGAC
GGAGCAGCCATCTTCCAGTGTGTGGCCGCGGTGTTCATTGCGCAACTCAACAACATAGAG
CTCAACGCAGGACAGATTTTCACCATTCTAGTGACTGCCACAGCGTCCAGTGTTGGAGCA
GCAGGCGTGCCAGCTGGAGGGGTCCTCACCATTGCCATTATCCTGGAGGCCATTGGGCTG
CCTACTCATGACCTGCCTCTGATCCTGGCTGTGGACTGGATTGTGGACCGGACCACCACG
GTGGTGAATGTGGAAGGGGATGCCCTGGGTGCAGGCATTCTCCACCACCTGAATCAGAAG
GCAACAAAGAAAGGCGAGCAGGAACTTGCTGAGGTGAAAGTGGAAGCCATCCCCAACTGC
AAGTCTGAGGAGGAGACATCGCCCCTGGTGACACACCAGAACCCCGCTGGCCCCGTGGCC
AGTGCCCCAGAACTGGAATCCAAGGAGTCGGTTCTGTGA
Enzyme 2 GenBank Gene ID L14595 Link Image
Enzyme 2 GeneCard ID SLC1A4 Link Image
Enzyme 2 GenAtlas ID SLC1A4 Link Image
Enzyme 2 HGNC ID HGNC:10942 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p15-p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Arriza JL, Kavanaugh MP, Fairman WA, Wu YN, Murdoch GH, North RA, Amara SG: Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family. J Biol Chem. 1993 Jul 25;268(21):15329-32. [PubMed Link Image]
  2. Shafqat S, Tamarappoo BK, Kilberg MS, Puranam RS, McNamara JO, Guadano-Ferraz A, Fremeau RT Jr: Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters. J Biol Chem. 1993 Jul 25;268(21):15351-5. [PubMed Link Image]
  3. Hofmann K, Duker M, Fink T, Lichter P, Stoffel W: Human neutral amino acid transporter ASCT1: structure of the gene (SLC1A4) and localization to chromosome 2p13-p15. Genomics. 1994 Nov 1;24(1):20-6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 8882
Enzyme 3 Name Threonine synthase-like 1
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name THNSL1
Enzyme 3 Protein Sequence >Threonine synthase-like 1 
MLHFNRCHHLKKITQKCFSSIHVKTDKHAQRFLSRTFALAELRKSWYSTHSLVGDKNIIL
MGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSVSEKLQDVGNEQFLEEEGKAVL
NFSASGSVISLTGSNPMHDASMWHLKKNGIIVYLDVPLLDLICRLKLMKTDRIVGQNSGT
SMKDLLKFRRQYYKKWYDARVFCESGASPEEVADKVLNAIKRYQDVDSETFISTRHVWPE
DCEQKVSAKFFSEAVIEGLASDGGLFVPAKEFPKLSCGEWKSLVGATYVERAQILLERCI
HPADIPAARLGEMIETAYGENFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPH
IFAHCIPPSCNYMILVATSGDTGSAVLNGFSRLNKNDKQRIAVVAFFPENGVSDFQKAQI
IGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTGFLTVEYGTILSSANSINWGRLLPQV
VYHASAYLDLVSQGFISFGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNHVL
TDFIKTGHYDLRERKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNRLESQHHF
QIEKALVEKLQQDFVADWCSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQDKTCPV
IISSTAHYSKFAPAIMQALKIKEINETSSSQLYLLGSYNALPPLHEALLERTKQQEKMEY
QVCAADMNVLKSHVEQLVQNQFI
Enzyme 3 Number of Residues 743
Enzyme 3 Molecular Weight 83071
Enzyme 3 Theoretical pI 7.13
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • carbon-oxygen lyase activity
  • carbon-oxygen lyase activity, acting on phosphates
  • catalytic activity
  • kinase activity
  • lyase activity
  • nucleotide binding
  • purine nucleotide binding
  • shikimate kinase activity
  • threonine synthase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • amino acid and derivative metabolism
  • amino acid biosynthesis
  • amino acid metabolism
  • aspartate family amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • threonine biosynthesis
  • threonine metabolism
Component
—
Enzyme 3 General Function Cell wall/membrane/envelope biogenesis
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals Not Available
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID Q8IYQ7 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name THNSL_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID BC035132 Link Image
Enzyme 3 GeneCard ID THNSL1 Link Image
Enzyme 3 GenAtlas ID THNSL1 Link Image
Enzyme 3 HGNC ID HGNC:26160 Link Image
Enzyme 3 Chromosome Location 10
Enzyme 3 Locus 10p12.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 13009
Enzyme 4 Name ILVBL protein
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name ILVBL
Enzyme 4 Protein Sequence >ILVBL protein 
VVTKKLLHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTR
HEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQN
RGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPY
FMVQKEMVPAKPPKGLVGRVVSWYLENYLANLFAGAWEPQPEGPLPLDIPQASPQQLLSN
N
Enzyme 4 Number of Residues 241
Enzyme 4 Molecular Weight 25613
Enzyme 4 Theoretical pI 10.17
Enzyme 4 GO Classification
Function
  • binding
  • thiamin pyrophosphate binding
  • vitamin binding
Process
—
Component
—
Enzyme 4 General Function Amino acid transport and metabolism
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 119850829 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID A1L0T0 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name A1L0T0_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence Not Available
Enzyme 4 GenBank Gene ID BC126913 Link Image
Enzyme 4 GeneCard ID A1L0T0 Link Image
Enzyme 4 GenAtlas ID ILVBL Link Image
Enzyme 4 HGNC ID HGNC:6041 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 13056
Enzyme 5 Name cDNA FLJ75173, highly similar to Homo sapiens threonyl-tRNA synthetase, mRNA
Enzyme 5 Synonyms
  1. Threonyl-tRNA synthetase, isoform CRA_b
Enzyme 5 Gene Name TARS
Enzyme 5 Protein Sequence >cDNA FLJ75173, highly similar to Homo sapiens threonyl-tRNA synthetase, mRNA 
MFEEKASSPSGKMGGEEKPIGAGEEKQKEGGKKKNKEGSGDGGRAELNPWPEYIYTRLEM
YNILKAEHDSILAEKAEKDSKPIKVTLPDGKQVDAESWKTTPYQIACGISQGLADNTVIA
KVNNVVWDLDRPLEEDCTLELLKFEDEEAQAVYWHSSAHIMGEAMERVYGGCLCYGPPIE
NGFYYDMYLEEGGVSSNDFSSLEALCKKIIKEKQAFERLEVKKETLLAMFKYNKFKCRIL
NEKVNTPTTTVYRCGPLIDLCRGPHVRHTGKIKALKIHKNSSTYWEGKADMETLQRIYGI
SFPDPKMLKEWEKFQEEAKNRDHRKIGRDQELYFFHELSPGSCFFLPKGAYIYNALIEFI
RSEYRKRGFQEVVTPNIFNSRLWMTSGHWQHYSENMFSFEVEKELFALKPMNCPGHCLMF
DHRPRSWRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCAMEQIEDEIKGCL
DFLRTVYSVFGFSFKLNLSTRPEKFLGDIEVWDQAEKQLENSLNEFGEKWELNSGDGAFY
GPKIDIQIKDAIGRYHQCATIQLDFQLPIRFNLTYVSHDGDDKKRPVIVHRAILGSVERM
IAILTENYGGKWPFWLSPRQVMVVPVGPTCDEYAQKVRQQFHDAKFMADIDLDPGCTLNK
KIRNAQLAQYNFILVVGEKEKISGTVNIRTRDNKVHGERTISETIERLQQLKEFRSKQAE
EEF
Enzyme 5 Number of Residues 723
Enzyme 5 Molecular Weight 83436
Enzyme 5 Theoretical pI 6.64
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Translation, ribosomal structure and biogenesis
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function Not Available
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 158258124 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID A8K8I1 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name A8K8I1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence Not Available
Enzyme 5 GenBank Gene ID AK292346 Link Image
Enzyme 5 GeneCard ID A8K8I1 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15074
Enzyme 6 Name Probable threonyl-tRNA synthetase 2, cytoplasmic
Enzyme 6 Synonyms
  1. Threonine--tRNA ligase
  2. ThrRS
  3. Threonyl-tRNA synthetase-like protein 2
Enzyme 6 Gene Name TARSL2
Enzyme 6 Protein Sequence >Probable threonyl-tRNA synthetase 2, cytoplasmic 
MAAEALAAEAVASRLERQEEDIRWLWSEVERLRDEQLNAPYSCQAEGPCLTREVAQLRAE
NCDLRHRLCSLRLCLAEERSRQATLESAELEAAQEAGAQPPPSQSQDKDMKKKKMKESEA
DSEVKHQPIFIKERLKLFEILKKDHQLLLAIYGKKGDTSNIITVRVADGQTVQGEVWKTT
PYQVAAEISQELAESTVIAKVNGELWDLDRPLEGDSSLELLTFDNEEAQAVYWHSSAHIL
GEAMELYYGGHLCYGPPIENGFYYDMFIEDRAVSSTELSALENICKAIIKEKQPFERLEV
SKEILLEMFKYNKFKCRILNEKVNTATTTVYRCGPLIDLCKGPHVRHTGKIKTIKIFKNS
STYWEGNPEMETLQRIYGISFPDNKMMRDWEKFQEEAKNRDHRKIGKEQELFFFHDLSPG
SCFFLPRGAFIYNTLTDFIREEYHKRDFTEVLSPNMYNSKLWEASGHWQHYSENMFTFEI
EKDTFALKPMNCPGHCLMFAHRPRSWREMPIRFADFGVLHRNELSGTLSGLTRVRRFQQD
DAHIFCTVEQIEEEIKGCLQFLQSVYSTFGFSFQLNLSTRPENFLGEIEMWNEAEKQLQN
SLMDFGEPWKMNPGDGAFYGPKIDIKIKDAIGRYHQCATIQLDFQLPIRFNLTYVSKDGD
DKKRPVIIHRAILGSVERMIAILSENYGGKWPFWLSPRQVMVIPVGPTCEKYALQVSSEF
FEEGFMADVDLDHSCTLNKKIRNAQLAQYNFILVVGEKEKIDNAVNVRTRDNKIHGEILV
TSAIDKLKNLRKTRTLNAEEAF
Enzyme 6 Number of Residues 802
Enzyme 6 Molecular Weight 92647
Enzyme 6 Theoretical pI 5.93
Enzyme 6 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
  • threonine-tRNA ligase activity
  • transition metal ion binding
  • transporter activity
Process
  • RNA metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • protein biosynthesis
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
  • threonyl-tRNA aminoacylation
Component
—
Enzyme 6 General Function Translation, ribosomal structure and biogenesis
Enzyme 6 Specific Function ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 16552114 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID A2RTX5 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name SYTC2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2124 bp 
ATGGCGGCCGAGGCCCTGGCGGCGGAGGCCGTGGCGTCGCGCCTGGAGCGGCAGGAGGAG
GACATCCGCTGGCTGTGGTCGGAGGTCGAGCGCCTGAGGGACGAGCAGCTGAACGCGCCC
TACAGCTGCCAGGCGGAGGGGCCGTGCCTCACGCGGGAGGTGGCGCAGCTCCGGGCCGAG
AACTGCGACCTGCGCCACCGCCTGTGCAGCCTGCGGCTGTGCCTCGCCGAGGAGCGGAGC
CGCCAGGCCACGCTGGAGAGCGCGGAGCTAGAGGCGGCGCAGGAGGGCGGCGCACAGCCT
CCTCCTAGTCAAAGCCAAGACAAGGACATGAAAAAGAAGAAAATGAAGGAAAGCGAGGCT
GACAGCGAGGTGAAGCATCAACCAATTTTCATAAAAGAAAGATTGAAGCTTTTTGAAATA
CTGAAGAAAGACCATCAGCTCTTACTTGCCATTTATGGAAAAAAGGGGGATACAAGCAAC
ATCATCACAGTAAGAGCGGCTGATGGGCAAACAGTGCAAGGGGAAGTCTGGAAAACAACG
CCTTACCAAGTGGCTGCTGAAATTAGTCAGGAACTGGCTGAAAGCACGGTAATAGCCAAA
GTCAATGGTGAACTGTGGGACCTGGACTGCCCATTGGAAGGGGACTCTTCTCTAGAGCTG
CTTACATTTGATAATGAGAAAGTTAACACTGCAACTACCACCGTGTACAGGTGCGGTCCA
TTAATTGACCTTTGCAAAGGTCCACATGTAAGACACACTGGAAAAATTAAAACCATCAAA
ATTTTTAAGAATTCCTCAACATATTGGGAGGGCAATCCGGAAATGGAAACATTGCAGAGG
ATCTATGGAATATCCTTTCCTGATAACAAGATGATGAGAGACTGGGAAAAGTTCCAAGAG
GAAGCAAAGAACCGAGATCACAGGAAGATCGGGAAGGAACAAGAACTTTTCTTTTTCCAC
GATTTGAGTCCTGGAAGCTGTTTTTTCCTTCCCAGAGGAGCCTTCATTTATAATACGCTT
ACAGATTTCATACGAGAGGAATATCACAAACGGGACTTCACGGAGGTGCTCTCTCCCAAT
ATGTACAACAGTAAACTCTGGGAAGCCTCAGGCCACTGGCAGCATTACAGCGAGAACATG
TTTACCTTTGAGATTGAAAAGGACACTTTTGCCCTCAAACCCATGAATTGTCCAGGGCAC
TGTCTAATGTTTGCCCATCGTCCACGATCTTGGAGGGAAATGCCTATTAGATTTGCTGAT
TTTGGAGTTCTGCATAGAAATGAACTGTCGGGGACTCTCAGTGGCTTGACCAGAGTGAGG
CGCTTCCAGCAGGACGATGCTCACATTTTTTGCACAGTGGAGCAGATTGAAGAAGAAATA
AAGGGGTGTTTGCAGTTTTTGCAATCTGTTTACTCAACATTTGGCTTCTCCTTTCAATTA
AACCTGTCAACAAGGCCGGAAAACTTCCTAGGAGAGATTGAGATGTGGAATGAGGCTGAG
AAGCAACTGCAGAACAGCTTGATGGACTTTGGAGAACCGTGGAAAATGAACCCAGGAGAT
GGAGCATTTTATGGCCCTAAAATTGACATAAAAATCAAGGATGCTATTGGCAGATACCAT
CAATGTGCTACAATTCAGCTGGACTTCCAACTGCCTATTAGATTTAATCTCACATATGTT
AGTAAGGATGGGGATGATAAGAAGAGACCTGTGATCATTCATCGAGCCATTTTGGGATCA
GTGGAAAGAATGATAGCCATTCTTTCAGAAAACTATGGCGGAAAATGGCCTTTCTGGCTA
TCTCCTCGTCAGGTGATGGTCATCCCTGTGGGGCCAACTTGTGAAAAATATGCACTTCAG
GTATCCAGTGAATTTTTTGAAGAAGGATTTATGGCTGACGTTGACTTGGATCACAGTTGT
ACACTAAATAAGAAAATACGAAATGCACAGCTGGCTCAGTATAATTTTATTTTGGTGGTT
GGAGAAAAGGAAAAGATAGATAATGCTGTAAACGTGCGAACAAGAGACAACAAAATTCAT
GGAGAGATTTTAGTAACTTCTGCCATTGATAAACTGAAGAATCTCAGGAAGACACGGACA
CTCAATGCTGAGGAGGCCTTTTGA
Enzyme 6 GenBank Gene ID AK056653 Link Image
Enzyme 6 GeneCard ID A2RTX5 Link Image
Enzyme 6 GenAtlas ID TARSL2 Link Image
Enzyme 6 HGNC ID HGNC:24728 Link Image
Enzyme 6 Chromosome Location 15
Enzyme 6 Locus 15q26.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15075
Enzyme 7 Name Threonyl-tRNA synthetase, mitochondrial
Enzyme 7 Synonyms
  1. Threonine--tRNA ligase
  2. ThrRS
  3. Threonyl-tRNA synthetase-like 1
Enzyme 7 Gene Name TARS2
Enzyme 7 Protein Sequence >Threonyl-tRNA synthetase, mitochondrial 
MALYQRWRCLRLQGLQACRLHTAVVSTPPRWLAERLGLFEELWAAQVKRLASMAQKEPRT
IKISLPGGQKIDAVAWNTTPYQLARQISSTLADTAVAAQVNGEPYDLERPLETDSDLRFL
TFDSPEGKAVFWHSSTHVLGAAAEQFLGAVLCRGPSTEYGFYHDFFLGKERTIRGSELPV
LERICQELTAAARPFRRLEASRDQLRQLFKDNPFKLHLIEEKVTGPTATVYGCGTLVDLC
QGPHLRHTGQIGGLKLLSNSSSLWRSSGAPETLQRVSGISFPTTELLRVWEAWREEAELR
DHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYAHRGFSEVKTPTLFSTK
LWEQSGHWEHYQEDMFAVQPPGSDRPPSSQSDDSTRHITDTLALKPMNCPAHCLMFAHRP
RSWRELPLRLADFGALHRAEASGGLGGLTRLRCFQQDDAHIFCTTDQLEAEIQSCLDFLR
SVYAVLGFSFRLALSTRPSGFLGDPCLWDQAEQVLKQALKEFGEPWDLNSGDGAFYGPKI
DVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGQAGALERPVLIHRAVLGSVERLLGVLA
ESCGGKWPLWLSPFQVVVIPVGSEQEEYAKEAQQSLRAAGLVSDLDADSGLTLSRRIRRA
QLAHYNFQFVVGQKEQSKRTVNIRTRDNRRLGEWDLPEAVQRLVELQNTRVPNAEEIF
Enzyme 7 Number of Residues 718
Enzyme 7 Molecular Weight 81037
Enzyme 7 Theoretical pI 7.31
Enzyme 7 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
  • threonine-tRNA ligase activity
  • transition metal ion binding
  • transporter activity
Process
  • RNA metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • protein biosynthesis
  • tRNA aminoacylation
  • tRNA aminoacylation for protein translation
  • tRNA metabolism
  • threonyl-tRNA aminoacylation
Component
—
Enzyme 7 General Function Translation, ribosomal structure and biogenesis
Enzyme 7 Specific Function ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 62897187 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9BW92 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name SYTM_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2157 bp 
ATGGCCCTGTATCAGAGGTGGCGGTGTCTCCGGCTCCAAGGTTTACAGGCTTGCAGGCTA
CACACGGCAGTTGTGTCGACCCCTCCACGCTGGTTGGCAGAGCGGCTTGGCCTTTTTGAG
GAGCTGTGGGCTGCTCAGGTAAAGAGATTAGCAAGCATGGCACAGAAGGAACCCCGGACT
ATTAAGATATCACTTCCTGGAGGCCAGAAAATTGATGCTGTGGCATGGAACACAACCCCC
TACCAACTAGCCCGGCAGATCAGTTCAACACTGGCAGATACTGCAGTGGCTGCTCAAGTG
AATGGAGAACCTTATGATCTGGAGCGGCCCTTGGAGACAGATTCTGACCTCAGATTTCTG
ACATTCGATTCCCCAGAGGGGAAAGCAGTGTTCTGGCACTCCAGCACCCATGTCCTGGGG
GCAGCAGCTGAACAATTCCTAGGTGCTGTTCTCTGCAGAGGTCCAAGTACAGAATATGGC
TTTTACCATGATTTCTTCCTGGGAAAGGAGAGGACAATCCGGGGCTCAGAGCTGCCTGTT
TTGGAGCGGATTTGCCAGGAACTTACAGCTGCTGCTCGACCCTTCCGGAGGCTAGAGGCT
TCACGGGATCAGCTTCGCCAGTTGTTCAAGGATAACCCCTTTAAGCTTCACTTGATTGAG
GAGAAAGTGACAGGTCCAACAGCAACAGTATATGGGTGTGGCACATTGGTTGACCTTTGC
CAGGGCCCCCACCTTCGGCATACTGGACAGATTGGAGGACTGAAGCTGCTATCGAACTCA
TCATCCTTATGGAGGTCTTCAGGGCCCCCAGAGACACTGCAGAGAGTGTCAGGGATTTCC
TTCCCCACAACAGAATTGCTGAGGGTCTGGGAAGCATGGAGGGAGGAAGCAGAATTGCGG
GACCACCGGCGCATTGGGAAGGAACAGGAGCTCTTCTTCTTCCATGAACTGAGCCCTGGG
AGCTGCTTCTTCCTGCCACGAGGGACAAGGGTGTATAATGCACTAGTGGCGTTTATCAGG
GCTGAGTATGCCCATCGTGGTTTCTCCGAGGTGAAAACTCCCACACTGTTTTCTACGAAG
CTCTGGGAACAGTCAGGGCACTGGGAGCATTATCAGGAAGACATGTTTGCCGTGCAGCCC
CCAGGCTCTGACAGGCCTCCCAGCTCCCAGAGTGACGATTCTACCAGGCATATCACAGAT
ACACTCGCCCTCAAGCCTATGAACTGCCCTGCACACTGCCTGATGTTCGCCCACCGGCCC
AGATCCTGGCGGGAACTGCCCCTGCGACTAGCTGACTTTGGGGCTCTACACCGGGCCGAA
GCCTCTGGTGGTCTGGGGGGACTGACCCGACTGCGGTGCTTCCAGCAGGATGACGCTCAC
ATCTTCTGTACAACAGATCAGCTGGAAGCAGAGATCCAAAGCTGTCTTGATTTCCTCCGT
TCCGTCTATGCCGTTCTTGGCTTCTCCTTCCGCCTGGCACTGTCCACCCGGCCATCTGGC
TTCCTGGGGGACCCTTGCCTTTGGGACCAGGCCGAACAGGTCCTTAAACAGGCCCTGAAG
GAATTTGGAGAACCCTGGGACCTCAACTCTGGAGATGGTGCCTTCTATGGACCTAAGATT
GACGTGCACCTCCACGATGCCCTGGGCCGGCCACATCAGTGTGGGACAATTCAGCTTGAC
TTCCAACTGCCCCTGAGATTTGACCTCCAGTATAAGGGGCAGGCGGGTGCCCTGGGGCGT
CCAGTCCTCATTCACCGAGCAGTGCTCGGTTCTGTGGAAAGACTGTTGGGAGTGCTGGCA
GAAAGCTGCGGGGGGAAATGGCCACTGTGGCTGTCCCCGTTCCAGGTGGTGGTCATCCCT
GTGGGGAGTGAGCAAGAGGAATACGCCAAAGAGGCACAGCAGAGCCTGCGGGCTGCAGGA
CTGGTCAGTGACCTGGATGCAGACTCTGGACTGACCCTCAGCCGGAGAATCCGCCGGGCC
CAGCTTGCCCACTACAATTTTCAGTTTGTGGTTGGCCAGAAAGAGCAAAGTAAGAGAACA
GTGAACATTCGGACTCGAGATAATCGTCGCCTTGGGGAGTGGGACTTGCCTGAGGCTGTG
CAGCGACTGGTGGAGCTACAGAACACGAGGGTCCCAAATGCCGAAGAAATTTTCTGA
Enzyme 7 GenBank Gene ID AK222814 Link Image
Enzyme 7 GeneCard ID Q9BW92 Link Image
Enzyme 7 GenAtlas ID TARS2 Link Image
Enzyme 7 HGNC ID HGNC:30740 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available