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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Histidine (HMDB00177)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-09-09 09:41:31
Accession Number HMDB00177
Secondary Accession Numbers HMDB03412
Common Name L-Histidine
Description Histidine is an essential amino acid for infants but not adults. Infants four to six months old require 33 mg/kg of histidine. It is not clear how adults make small amounts of histidine, and dietary sources probably account for most of the histidine in the body. Inborn errors of histidine metabolism exist and are marked by increased histidine levels in the blood. Elevated blood histidine is accompanied by a wide range of symptoms, from mental and physical retardation to poor intellectual functioning, emotional instability, tremor, ataxia and psychosis. Histidine in medical therapies has its most promising trials in rheumatoid arthritis where up to 4.5 g daily have been used effectively in severely affected patients. Arthritis patients have been found to have low serum histidine levels, apparently because of too-rapid removal of histidine from their blood. Histidine and other imidazole compounds have anti-inflammatory properties. histidine may accomplish this function through a complex interaction with threonine or cysteine and possibly copper. However, copper is usually elevated in rheumatoid arthritis patients and worsens the disease. Other patients besides arthritis patients that have been found to be low in serum histidine are those with chronic renal failure. Histidine has been claimed to have been useful in hypertension because of its vasodilatory effects. Claims of its use to improve libido and counteract allergy are without proof at present. Histidine may have many other possible functions because it is the precursor of the ubiquitous neurohormone-neurotransmitter histamine. Histidine increases histamine in the blood and probably in the brain. Low blood histamine with low serum histidine occurs in rheumatoid arthritis patients. Low blood histamine also occurs in some manic, schizophrenic, high copper and hyperactive groups of psychiatric patients. Histidine is a useful therapy in all low histamine patients. ( http://www.dcnutrition.com )
Synonyms
  1. (S)-1H-Imidazole-4-alanine
  2. (S)-2-Amino-3-(4-imidazolyl)propionsaeure
  3. (S)-4-(2-Amino-2-carboxyethyl)imidazole
  4. (S)-Histidine
  5. (S)-a-Amino-1H-imidazole-4-propanoate
  6. (S)-a-Amino-1H-imidazole-4-propanoic acid
  7. (S)-alpha-Amino-1H-imidazole-4-propanoate
  8. (S)-alpha-Amino-1H-imidazole-4-propanoic acid
  9. (S)-alpha-Amino-1H-imidazole-4-propionate
  10. (S)-alpha-Amino-1H-imidazole-4-propionic acid
  11. (S)1H-Imidazole-4-alanine
  12. 3-(1H-imidazol-4-yl)-L-Alanine
  13. Glyoxaline-5-alanine
  14. His
  15. Histidine
  16. L-(-)-Histidine
  17. amino-1H-imidazole-4-propanoate
  18. amino-1H-imidazole-4-propanoic acid
  19. amino-4-imidazoleproprionate
  20. amino-4-imidazoleproprionic acid
Chemical IUPAC Name 2-amino-3-(3H-imidazol-4-yl)propanoic acid
Chemical Formula C6H9N3O2
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
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
  • alpha-aminoacid
Biofunction
  • Essential amino acids
  • semi-essential amino acids
  • Essential amino acid
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Histidine metabolism
  • Component of Nitrogen metabolism
Application
—
Source
  • Exogenous
Average Molecular Weight 155.155
Monoisotopic Molecular Weight 155.069473
Isomeric SMILES N[C@@H](CC1=CNC=N1)C(O)=O
Canonical SMILES NC(CC1=CNC=N1)C(O)=O
KEGG Compound ID C00135 Link Image
BioCyc ID HIS Link Image
BiGG ID 33985 Link Image
Wikipedia Link L-Histidine Link Image
NuGOwiki Link HMDB00177 Link Image
Metagene Link HMDB00177 Link Image
METLIN ID 21 Link Image
PubChem Compound 6274 Link Image
PubChem Substance 8023160 Link Image
ChEBI ID 15971 Link Image
CAS Registry Number 71-00-1
InChI Identifier InChI=1/C6H9N3O2/c7-5(6(10)11)1-4-2-8-3-9-4/h2-3,5H,1,7H2,(H,8,9)(H,10,11)/t5-/m0/s1
Synthesis Reference Aurelio Luigi; Brownlee Robert T C; Hughes Andrew B A novel synthesis of N-methyl asparagine, arginine, histidine, and tryptophan. Organic letters (2002), 4(21), 3767-9.
Melting Point (Experimental) 287 oC
Experimental Water Solubility 45.6 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)] Source: PhysProp
Predicted Water Solubility 71.3 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity -3.32 [CHMELIK,J ET AL. (1991)] Source: PhysProp
Predicted LogP/Hydrophobicity -2.67 [Predicted by ALOGPS]; -3.4 [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 1KAH 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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Saliva
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Blood
Value 82.0 (72.0-92.0) 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 75.0 +/- 20.0 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 86.0 +/- 10.0 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 89.0 +/- 11.0 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 83.0 +/- 14.0 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 88.00 (56.00-120.00) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid CSF
Value 11.9 +/- 1.7 uM
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 10.9 (10.4-11.4) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
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 CSF
Value 20.7 +/- 7.5 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 16.8 +/- 2.7 uM
Age Adult:>18 yrs old
Sex Male
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 18.6 +/- 3.3 uM
Age Adult:>18 yrs old
Sex Female
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 14.0 +/- 8.0 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Knox C, Guo AC, Eisner R, Young N, Gautam B, Hau DD, Psychogios N, Dong E, Bouatra S, Mandal R, Sinelnikov I, Xia J, Jia L, Cruz JA, Lim E, Sobsey CA, Shrivastava S, Huang P, Liu P, Fang L, Peng J, Fradette R, Cheng D, Tzur D, Clements M, Lewis A, De Souza A, Zuniga A, Dawe M, Xiong Y, Clive D, Greiner R, Nazyrova A, Shaykhutdinov R, Li L, Vogel HJ, Forsythe I: HMDB: a knowledgebase for the human metabolome. Nucleic Acids Res. 2008 Oct 25. [PubMed Link Image]
Biofluid CSF
Value 13.00 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
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 194.90 +/- 144.31 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 87.2 (23.0-151.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 2.2 (1.18-3.4) 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 31.0 +/- 15.0 umol/mmol creatinine
Age Children:1-13 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 85.0 +/- 33.0 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 62.0 +/- 28.0 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 101.9 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]
Biofluid Urine
Value 659 +/- 64 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Biofluid Urine
Value 112.00 (59.00-166.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Blood
Value 67.0 (64.0-70.0) uM
Age Adult:>18 yrs old
Sex Both
Condition Dengue fever
Comments Not Available
References
  • Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52. [PubMed Link Image]
Biofluid Blood
Value 80.5 +/- 4.2 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 107.0 +/- 6.5 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 116.68 +/- 18.15 uM
Age Elderly:>65 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]
Biofluid Blood
Value 885.00 (290.00-1420.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Histidinemia
Comments Not Available
References
Biofluid CSF
Value 130.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Histidinemia
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 21.4 +/- 6.6 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 10.3 +/- 3.7 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 14.4 +/- 6.32 uM
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]
Biofluid CSF
Value 95.00 (48.00-142.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Histidinemia
Comments Not Available
References
Biofluid Urine
Value 30.5 +/- 4.3 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]
Dengue fever
  • Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52. [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]
Histidinemia
  • 7729054
  • http://www.metagene.de/program/d.prg?mp=HISTIDINEMIA
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]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Histidine Metabolism SMP00044 Link Image map00340 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Mukerji SK, Pimstone NR, Gandhi SN, Tan KT: Biochemical diagnosis and monitoring therapeutic modulation of disease activity in an unusual case of congenital erythropoietic porphyria. Clin Chem. 1985 Dec;31(12):1946-51. [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. 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]
  4. 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]
  5. Xiao B, Jing C, Kelly G, Walker PA, Muskett FW, Frenkiel TA, Martin SR, Sarma K, Reinberg D, Gamblin SJ, Wilson JR: Specificity and mechanism of the histone methyltransferase Pr-Set7. Genes Dev. 2005 Jun 15;19(12):1444-54. Epub 2005 Jun 2. [PubMed Link Image]
  6. Churchill D, Yacoub JM, Siu KP, Symes A, Gault MH: Toxic nephropathy after low-dose methoxyflurane anesthesia: drug interaction with secobarbital? Can Med Assoc J. 1976 Feb 21;114(4):326-8, 333. [PubMed Link Image]
  7. 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]
  8. Sieja K, Stanosz S, von Mach-Szczypinski J, Olewniczak S, Stanosz M: Concentration of histamine in serum and tissues of the primary ductal breast cancers in women. Breast. 2005 Jun;14(3):236-41. Epub 2005 Jan 21. [PubMed Link Image]
  9. 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]
  10. 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]
  11. Masini E, Fabbroni V, Giannini L, Vannacci A, Messerini L, Perna F, Cortesini C, Cianchi F: Histamine and histidine decarboxylase up-regulation in colorectal cancer: correlation with tumor stage. Inflamm Res. 2005 Apr;54 Suppl 1:S80-1. [PubMed Link Image]
  12. Klassen P, Furst P, Schulz C, Mazariegos M, Solomons NW: Plasma free amino acid concentrations in healthy Guatemalan adults and in patients with classic dengue. Am J Clin Nutr. 2001 Mar;73(3):647-52. [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. Xiao YP, Han CB, Mao XY, Li JY, Xu L, Ren CS, Xin Y: Relationship between abnormality of FHIT gene and EBV infection in gastric cancer. World J Gastroenterol. 2005 Jun 7;11(21):3212-6. [PubMed Link Image]
  15. Mason AB, Halbrooks PJ, James NG, Connolly SA, Larouche JR, Smith VC, MacGillivray RT, Chasteen ND: Mutational analysis of C-lobe ligands of human serum transferrin: insights into the mechanism of iron release. Biochemistry. 2005 Jun 7;44(22):8013-21. [PubMed Link Image]
  16. Janknecht R, Hipskind RA, Houthaeve T, Nordheim A, Stunnenberg HG: Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties. EMBO J. 1992 Mar;11(3):1045-54. [PubMed Link Image]
  17. 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]
  18. Wikipedia Link Image
Metabolic Enzymes
  1. Aromatic-L-amino-acid decarboxylase
  2. Beta-Ala-His dipeptidase precursor
  3. Protein arginine N-methyltransferase 3
  4. Probable histidyl-tRNA synthetase, mitochondrial precursor
  5. Histidyl-tRNA synthetase, cytoplasmic
  6. Histidine ammonia-lyase
  7. Histidine decarboxylase
  8. System N amino acid transporter 1
  9. Solute carrier family 38, member 3, isoform CRA_b
Enzyme 1 [top]
Enzyme 1 ID 5510
Enzyme 1 Name Aromatic-L-amino-acid decarboxylase
Enzyme 1 Synonyms
  1. AADC
  2. DOPA decarboxylase
  3. DDC
Enzyme 1 Gene Name DDC
Enzyme 1 Protein Sequence >Aromatic-L-amino-acid decarboxylase 
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDV
EKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMD
WLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIM
EKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMV
ATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFN
PHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSL
KMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVN
EALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
Enzyme 1 Number of Residues 480
Enzyme 1 Molecular Weight 53895
Enzyme 1 Theoretical pI 7.21
Enzyme 1 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Amino acid transport and metabolism
Enzyme 1 Specific Function Catalyzes the decarboxylation of L-3,4- dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • L-tryptophan = tryptamine + CO2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 181521 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P20711 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DDC_HUMAN Link Image
Enzyme 1 PDB ID 1JS3 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1443 bp 
ATGAACGCAAGTGAATTCCGAAGGAGAGGGAAGGAGATGGTGGATTACGTGGCCAACTAC
ATGGAAGGCATTGAGGGACGCCAGGTCTACCCTGACGTGGAGCCCGGGTACCTGCGGCCG
CTGATCCCTGCCGCTGCCCCTCAGGAGCCAGACACGTTTGAGGACATCATCAACGACGTT
GAGAAGATAATCATGCCTGGGGTGACGCACTGGCACAGCCCCTACTTCTTCGCCTACTTC
CCCACTGCCAGCTCGTACCCGGCCATGCTTGCGGACATGCTGTGCGGGGCCATTGGCTGC
ATCGGCTTCTCCTGGGCGGCAAGCCCAGCATGCACAGAGCTGGAGACTGTGATGATGGAC
TGGCTCGGGAAGATGCTGGAACTACCAAAGGCATTTTTGAATGAGAAAGCTGGAGAAGGG
GGAGGAGTGATCCAGGGAAGTGCCAGTGAAGCCACCCTGGTGGCCCTGCTGGCCGCTCGG
ACCAAAGTGATCCATCGGCTGCAGGCAGCGTCCCCAGAGCTCACACAGGCCGCTATCATG
GAGAAGCTGGTGGCTTACTCATCCGATCAGGCACACTCCTCAGTGGAAAGAGCTGGGTTA
ATTGGTGGAGTGAAATTAAAAGCCATCCCCTCAGATGGCAACTTCGCCATGCGTGCGTCT
GCCCTGCAGGAAGCCCTGGAGAGAGACAAAGCGGCTGGCCTGATTCCTTTCTTTATGGTT
GCCACCCTGGGGACCACAACATGCTGCTCCTTTGACAATCTCTTAGAAGTCGGTCCTATC
TGCAACAAGGAAGACATATGGCTGCACGTTGATGCAGCCTACGCAGGCAGTGCATTCATC
TGCCCTGAGTTCCGGCACCTTCTGAATGGAGTGGAGTTTGCAGATTCATTCAACTTTAAT
CCCCACAAATGGCTATTGGTGAATTTTGACTGTTCTGCCATGTGGGTGAAAAAGAGAACA
GACTTAACGGGAGCCTTTAGACTGGACCCCACTTACCTGAAGCACAGCCATCAGGATTCA
GGGCTTATCACTGACTACCGGCATTGGCAGATACCACTGGGCAGAAGATTTCGCTCTTTG
AAAATGTGGTTTGTATTTAGGATGTATGGAGTCAAAGGACTGCAGGCTTATATCCGCAAG
CATGTCCAGCTGTCCCATGAGTTTGAGTCACTGGTGCGCCAGGATCCCCGCTTTGAAATC
TGTGTGGAAGTCATTCTGGGGCTTGTCTGCTTTCGGCTAAAGGGTTCCAACAAAGTGAAT
GAAGCTCTTCTGCAAAGAATAAACAGTGCCAAAAAAATCCACTTGGTTCCATGTCACCTC
AGGGACAAGTTTGTCCTGCGCTTTGCCATCTGTTCTCGCACGGTGGAATCTGCCCATGTG
CAGCGGGCCTGGGAACACATCAAAGAGCTGGCGGCCGACGTGCTGCGAGCAGAGAGGGAG
TAG
Enzyme 1 GenBank Gene ID M76180 Link Image
Enzyme 1 GeneCard ID DDC Link Image
Enzyme 1 GenAtlas ID DDC Link Image
Enzyme 1 HGNC ID HGNC:2719 Link Image
Enzyme 1 Chromosome Location 7
Enzyme 1 Locus 7p11
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Ichinose H, Kurosawa Y, Titani K, Fujita K, Nagatsu T: Isolation and characterization of a cDNA clone encoding human aromatic L-amino acid decarboxylase. Biochem Biophys Res Commun. 1989 Nov 15;164(3):1024-30. [PubMed Link Image]
  2. Scherer LJ, McPherson JD, Wasmuth JJ, Marsh JL: Human dopa decarboxylase: localization to human chromosome 7p11 and characterization of hepatic cDNAs. Genomics. 1992 Jun;13(2):469-71. [PubMed Link Image]
  3. Sumi-Ichinose C, Ichinose H, Takahashi E, Hori T, Nagatsu T: Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis. Biochemistry. 1992 Mar 3;31(8):2229-38. [PubMed Link Image]
  4. Le Van Thai A, Coste E, Allen JM, Palmiter RD, Weber MJ: Identification of a neuron-specific promoter of human aromatic L-amino acid decarboxylase gene. Brain Res Mol Brain Res. 1993 Mar;17(3-4):227-38. [PubMed Link Image]
  5. Craig SP, Thai AL, Weber M, Craig IW: Localisation of the gene for human aromatic L-amino acid decarboxylase (DDC) to chromosome 7p13-->p11 by in situ hybridisation. Cytogenet Cell Genet. 1992;61(2):114-6. [PubMed Link Image]
  6. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5713
Enzyme 2 Name Beta-Ala-His dipeptidase precursor
Enzyme 2 Synonyms
  1. Carnosine dipeptidase 1
  2. CNDP dipeptidase 1
  3. Serum carnosinase
  4. Glutamate carboxypeptidase-like protein 2
Enzyme 2 Gene Name CNDP1
Enzyme 2 Protein Sequence >Beta-Ala-His dipeptidase precursor 
MDPKLGRMAASLLAVLLLLLERGMFSSPSPPPALLEKVFQYIDLHQDEFVQTLKEWVAIE
SDSVQPVPRFRQELFRMMAVAADTLQRLGARVASVDMGPQQLPDGQSLPIPPVILAELGS
DPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAF
RALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAIT
YGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHILVPGIYDEVV
PLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFDEPG
TKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIA
NIDDTQYLAAKRAIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQ
NEKINRWNYIEGTKLFAAFFLEMAQLH
Enzyme 2 Number of Residues 507
Enzyme 2 Molecular Weight 56693
Enzyme 2 Theoretical pI 4.95
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • metallopeptidase activity
  • peptidase activity
  • protein binding
  • protein dimerization activity
Process
  • cellular protein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
—
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-26
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 16555792 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q96KN2 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CNDP1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1527 bp 
ATGGATCCCAAACTCGGGAGAATGGCTGCGTCCCTGCTGGCTGTGCTGCTGCTGCTGCTG
CTGGAGCGCGGCATGTTCTCCTCACCCTCCCCGCCCCCGGCGCTGTTAGAGAAAGTCTTC
CAGTACATTGACCTCCATCAGGATGAATTTGTGCAGACGCTGAAGGAGTGGGTGGCCATC
GAGAGCGACTCTGTCCAGCCTGTGCCTCGCTTCAGACAAGAGCTCTTCAGAATGATGGCC
GTGGCTGCGGACACGCTGCAGCGCCTGGGGGCCCGTGTGGCCTCGGTGGACATGGGTCCT
CAGCAGCTGCCCGATGGTCAGAGTCTTCCAATACCTCCCGTCATCCTGGCCGAACTGGGG
AGCGATCCCACGAAAGGCACCGTGTGCTTCTACGGCCACTTGGACGTGCAGCCTGCTGAC
CGGGGCGATGGGTGGCTCACGGACCCCTATGTGCTGACGGAGGTAGGCGGGAAACTTTAT
GGACGAGGAGCGACCGACAACAAAGGCCCTGTCTTGGCTTGGATCAATGCTGTGAGCGCC
TTCAGAGCCCTGGAGCAAGATCTTCCTGTGAATATCAAATTCATCATTGAGGGGATGGAA
GAGGCTGGCTCTGTTGCCCTGGAGGAACTTGTGGAAAAAGAAAAGGACCGATTCTTCTCT
GGTGTGGACTACATTGTAATTTCAGATAACCTGTGGATCAGCCAAAGGAAGCTAGCAATC
ACTTACGGAACCCGGGGGAACAGCTACTTCATGGTGGAGGTGAAATGCAGAGACCAGGAT
TTTCACTCAGGAACCTTTGGTGGCATCCTTCATGAACTAATGGCTGATCTGGTTGCTCTT
CTCGGTAGCCTGGTAGACTCGTCTGGTCATATCCTGGTCCCTGGAATCTATGATGAAGTG
GTTCCTCTTACAGAAGAGGAAATAAATACATACAAAGCCATCCATCTAGACCTAGAAGAA
TACCGGAATAGCAGCCGGGTTGAGAAATTTCTGTTCGATACTAAGGAGGAGATTCTAATG
CACCTCTGGAGGTACCCATCTCTTTCTATTCATGGGATCGAGGGCGCGTTTGATGAGCCT
GGAACTAAAACAGTCATACCTGGCCGAGTTATAGGAAAATTTTCAATCCGTCTAGTCCCT
CACATGAATGTGTCTGCGGTGGAAAAACAGGTGACACGACATCTTGAAGATGTGTTCTCC
AAAAGAAATAGTTCCAACAAGATGGTTGTTTCCATGACTCTAGGACTACACCCGTGGATT
GCAAATATTGATGACACTCAGTATCTCGCAGCAAAAAGAGCGATCAGAACAGTGTTTGGA
ACAGAACCAGATATGATCCGGGATGGATCCACCATTCCAATTGCCAAAATGTTCCAGGAG
ATCGTCCACAAGAGCGTGGTGCTAATTCCGCTGGGAGCTGTTGATGATGGAGAACATTCG
CAGAATGAGAAAATCAACAGGTGGAACTACATAGAGGGAACCAAATTATTTGCTGCCTTT
TTCTTAGAGATGGCCCAGCTCCATTAA
Enzyme 2 GenBank Gene ID AJ417564 Link Image
Enzyme 2 GeneCard ID CNDP1 Link Image
Enzyme 2 GenAtlas ID CNDP1 Link Image
Enzyme 2 HGNC ID HGNC:20675 Link Image
Enzyme 2 Chromosome Location 18
Enzyme 2 Locus 18q22.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5714
Enzyme 3 Name Protein arginine N-methyltransferase 3
Enzyme 3 Synonyms
  1. Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
Enzyme 3 Gene Name PRMT3
Enzyme 3 Protein Sequence >Protein arginine N-methyltransferase 3 
MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSA
EETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEY
LKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAR
EDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRT
ESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLN
KLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYP
DICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIK
HIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHW
KQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ
Enzyme 3 Number of Residues 531
Enzyme 3 Molecular Weight 59904
Enzyme 3 Theoretical pI 5.00
Enzyme 3 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • nucleic acid binding
  • transition metal ion binding
  • zinc ion binding
Process
—
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 45946104 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O60678 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ANM3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1596 bp 
ATGTGCTCGTTAGCGTCAGGCGCTACCGGCGGCCGGGGCGCTGTGGAGAATGAGGAGGAC
CTGCCAGAACTGTCGGACAGCGGGGACGAGGCCGCCTGGGAGGATGAGGACGATGCAGAT
CTCCCCCACGGCAAGCAGCAGACCCCCTGCCTGTTCTGTAACAGGTTATTCACATCTGCT
GAAGAAACATTTTCACACTGTAAGTCTGAGCATCAGTTTAATATTGACAGCATGGTTCAT
AAACATGGACTTGAATTTTATGGATACATTAAGCTAATAAATTTTATTAGACTTAAGAAT
CCTACAGTTGAGTACATGAATTCCATATACAACCCAGTGCCTTGGGAGAAAGAAGAGTAT
TTGAAGCCAGTATTAGAAGATGACCTTTTACTTCAATTTGATGTAGAAGATCTTTATGAA
CCGGTGTCAGTACCCTTCTCATACCCCAATGGACTCAGTGAAAATACATCTGTTGTTGAA
AAATTGAAACATATGGAAGCCAGGGCACTGTCTGCTGAAGCCGCATTGGCCAGAGCACGT
GAGGATCTGCAGAAAATGAAACAATTTGCTCAGGATTTTGTGATGCACACAGATGTCAGA
ACCTGCTCGTCATCTACTAGTGTCATTGCGGACCTCCAGGAGGATGAGGATGGTGTTTAT
TTCAGCTCATACGGGCATTATGGGATACATGAAGAAATGCTAAAGGACAAAATACGAACA
GAAAGCTACCGAGATTTCATATACCAAAATCCACATATCTTCAAAGACAAGGTAGTTTTG
GATGTTGGGTGTGGAACTGGAATTCTCTCTATGTTTGCTGCTAAAGCTGGGGCGAAGAAG
GTTCTTGGAGTTGATCAATCTGAAATACTTTACCAGGCAATGGATATTATAAGACTAAAT
AAACTTGAAGATACTATTACACTAATTAAAGGAAAGATTGAAGAAGTTCATCTTCCTGTA
GAAAAAGTAGATGTTATCATATCTGAGTGGATGGGCTATTTTCTTCTGTTTGAGTCTATG
TTAGATTCTGTCCTTTATGCAAAGAACAAATACTTGGCAAAAGGAGGCTCGGTCTACCCT
GACATTTGCACTATCAGCCTTGTAGCAGTGAGTGATGTGAATAAACATGCTGATAGAATT
GCTTTTTGGGATGATGTCTATGGCTTCAAGATGTCCTGCATGAAGAAAGCAGTTATTCCA
GAAGCTGTTGTGGAAGTTTTAGATCCGAAGACTCTTATTTCAGAACCTTGTGGTATTAAG
CATATAGATTGCCATACGACGTCTATCTCAGATTTGGAATTTTCATCAGATTTTACCCTG
AAAATCACAAGGACATCCATGTGCACGGCAATTGCTGGCTACTTTGATATATATTTTGAG
AAGAATTGCCACAACAGGGTCGTGTTCTCTACGGGCCCTCAGAGCACCAAAACACACTGG
AAACAAACAGTATTTCTACTGGAAAAACCATTTTCAGTTAAAGCAGGTGAAGCCTTGAAA
GGAAAGGTCACAGTTCACAAGAATAAGAAAGATCCACGTTCTCTCACCGTGACCCTCACG
TTGAATAATTCAACTCAAACTTATGGTCTCCAGTGA
Enzyme 3 GenBank Gene ID BC037544 Link Image
Enzyme 3 GeneCard ID PRMT3 Link Image
Enzyme 3 GenAtlas ID PRMT3 Link Image
Enzyme 3 HGNC ID HGNC:30163 Link Image
Enzyme 3 Chromosome Location 11
Enzyme 3 Locus 11p15.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Tang J, Gary JD, Clarke S, Herschman HR: PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J Biol Chem. 1998 Jul 3;273(27):16935-45. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5914
Enzyme 4 Name Probable histidyl-tRNA synthetase, mitochondrial precursor
Enzyme 4 Synonyms
  1. Histidine--tRNA ligase
  2. HisRS
  3. Histidine--tRNA ligase-like
Enzyme 4 Gene Name HARSL
Enzyme 4 Protein Sequence >Probable histidyl-tRNA synthetase, mitochondrial precursor 
MPLLGLLPRRAWASLLSQLLRPPCASCTGAVRCQSQVAEAVLTSQLKAHQEKPNFIIKTP
KGTRDLSPQHMVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKD
QGGELLSLRYDLTVPFARYLAMNKVKKMKRYHVGKVWRRESPTIVQGRYREFCQCDFDIA
GQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSID
KLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPRLSQNKQALEGL
GDLKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQAGEEPLNVGSVAA
GGRYDGLVGMFDPKGHKVPCVGLSIGVERIFYIVEQRMKTKGEKVRTTETQVFVATPQKN
FLQERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIR
SVASREEVAIKRENFVAEIQKRLSES
Enzyme 4 Number of Residues 506
Enzyme 4 Molecular Weight 56889
Enzyme 4 Theoretical pI 8.35
Enzyme 4 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • histidine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • histidyl-tRNA aminoacylation
  • 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
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 4 General Function Translation, ribosomal structure and biogenesis
Enzyme 4 Specific Function ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-13
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID P49590 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SYHM_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 U18936 Link Image
Enzyme 4 GeneCard ID HARSL Link Image
Enzyme 4 GenAtlas ID HARSL Link Image
Enzyme 4 HGNC ID HGNC:4817 Link Image
Enzyme 4 Chromosome Location 5
Enzyme 4 Locus 5q31.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. O'Hanlon TP, Raben N, Miller FW: A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS. Biochem Biophys Res Commun. 1995 May 16;210(2):556-66. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5917
Enzyme 5 Name Histidyl-tRNA synthetase, cytoplasmic
Enzyme 5 Synonyms
  1. Histidine--tRNA ligase
  2. HisRS
Enzyme 5 Gene Name HARS
Enzyme 5 Protein Sequence >Histidyl-tRNA synthetase, cytoplasmic 
MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPK
GTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQ
GGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAG
NFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDK
LDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDPKLSQNKQALEGLG
DLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAG
GRYDGLVGMFDPKGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKL
LEERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRS
VTSREEVDVRREDLVEEIKRRTGQPLCIC
Enzyme 5 Number of Residues 509
Enzyme 5 Molecular Weight 57411
Enzyme 5 Theoretical pI 5.56
Enzyme 5 GO Classification
Function
  • ATP binding
  • RNA ligase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • histidine-tRNA ligase activity
  • ligase activity
  • ligase activity, forming phosphoric ester bonds
  • nucleotide binding
  • purine nucleotide binding
  • tRNA ligase activity
Process
  • RNA metabolism
  • cellular metabolism
  • histidyl-tRNA aminoacylation
  • 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
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 5 General Function Translation, ribosomal structure and biogenesis
Enzyme 5 Specific Function ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 32460 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P12081 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SYHC_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1530 bp 
ATGGCAGAGCGTGCGGCGCTGGAGGAGCTGGTGAAACTTCAGGGAGAGCGCGTGCGAGGC
CTCAAGCAGCAGAAGGCCAGCGCCGAGCTGATCGAGGAGGAGGTGGCGAAACTCCTGAAA
CTGAAGGCACAGCTGGGTCCTGATGAAAGCAAACAGAAATTTGTGCTCAAAACCCCCAAG
GGCACAAGAGACTATAGTCCCCGGCAGATGGCAGTTCGCGAGAAGGTGTTTGACGTAATC
ATCCGTTGCTTCAAGCGCCACGGTGCAGAAGTCATTGATACACCTGTATTTGAACTAAAG
GAAACACTGATGGGAAAGTATGGGGAAGACTCCAAGCTTATCTATGACCTGAAGGACCAG
GGCGGGGAGCTCCTGTCCCTTCGCTATGACCTCACTGTTCCTTTTGCTCGGTATTTGGCA
ATGAATAAACTGACCAACATTAAACGCTACCACATAGCAAAGGTATATCGGCGGGATAAC
CCAGCCATGACCCGTGGCCGATACCGGGAATTCTACCAGTGTGATTTTGACATTGCTGGG
AACTTTGATCCCATGATCCCTGATGCAGAGTGCCTGAAGATCATGTGCGAGATCCTGAGT
TCACTTCAGATAGGCGACTTCCTGGTCAAGGTAAACGATCGACGCATTCTAGATGGGATG
TTTGCTATCTGTGGTGTTTCTGACAGCAAGTTCCGTACCATCTGCTCCTCAGTAGACAAG
CTGGACAAGGTGTCCTGGGAAGAGGTGAAGAATGAGATGGTGGGAGAGAAGGGCCTTGCA
CCTGAGGTGGCTGACCGCATTGGGGACTATGTCCAGCAACATGGTGGGGTATCCCTGGTG
GAACAGCTGCTCCAGGATCCTAAACTATCCCAAAACAAGCAGGCCTTGGAGGGCCTGGGA
GACCTGAAGTTGCTCTTTGAGTACCTGACCCTATTTGGCATTGATGACAAAATCTCCTTT
GACCTGAGCCTTGCTCGAGGGCTGGATTACTACACTGGGGTGATCTATGAGGCAGTGCTG
CTACAGACCCCAGCCCAGGCAGGGGAAGAGCCCCTGGGTGTGGGCAGTGTGGCTGCTGGA
GGACGCTATGATGGGCTAGTGGGCATGTTCGACCCCAAAGGGCGCAAGGTGCCATGTGTG
GGGCTCAGCATTGGGGTGGAGCGGATTTTCTCCATCGTGGAACAGAGACTAGAGGCTTTG
GAGGAGAAGATACGGACCACGGAGACACAGGTGCTTGTGGCATCTGCACAGAAGAAGCTG
CTAGAGGAAAGACTAAAGCTTGTCTCAGAACTGTGGGATGCTGGGATCAAGGCTGAGCTG
CTGTACAAGAAGAACCCAAAGCTACTGAACCAGTTACAGTACTGTGAGGAGGCAGGCATC
CCACTGGTGGCTATCATCGGCGAGCAGGAACTCAAGGATGGGGTCATCAAGCTCCGTTCA
GTGACGAGCAGGGAAGAGGTGGATGTCCGAAGAGAAGACCTTGTGGAGGAAATCAAAAGG
AGAACAGGCCAGCCCCTCTGCATCTGCTGA
Enzyme 5 GenBank Gene ID Z11518 Link Image
Enzyme 5 GeneCard ID HARS Link Image
Enzyme 5 GenAtlas ID HARS Link Image
Enzyme 5 HGNC ID HGNC:4816 Link Image
Enzyme 5 Chromosome Location 5
Enzyme 5 Locus 5q31.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Raben N, Borriello F, Amin J, Horwitz R, Fraser D, Plotz P: Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases. Nucleic Acids Res. 1992 Mar 11;20(5):1075-81. [PubMed Link Image]
  2. Tsui FW, Siminovitch L: Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase. Nucleic Acids Res. 1987 Apr 24;15(8):3349-67. [PubMed Link Image]
  3. Tsui HW, Mok S, de Souza L, Martin A, Tsui FW: Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element. Gene. 1993 Sep 15;131(2):201-8. [PubMed Link Image]
  4. O'Hanlon TP, Raben N, Miller FW: A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS. Biochem Biophys Res Commun. 1995 May 16;210(2):556-66. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5956
Enzyme 6 Name Histidine ammonia-lyase
Enzyme 6 Synonyms
  1. Histidase
Enzyme 6 Gene Name HAL
Enzyme 6 Protein Sequence >Histidine ammonia-lyase 
MPRYTVHVRGEWLAVPCQDAQLTVGWLGREAVRRYIKNKPDNGGFTSVDDAHFLVRRCKG
LGLLDNEDRLEVALENNEFVEVVIEGDAMSPDFIPSQPEGVYLYSKYREPEKYIELDGDR
LTTEDLVNLGKGRYKIKLTPTAEKRVQKSREVIDSIIKEKTVVYGITTGFGKFARTVIPI
NKLQELQVNLVRSHSSGVGKPLSPERCRMLLALRINVLAKGYSGISLETLKQVIEMFNAS
CLPYVPEKGTVGASGDLAPLSHLALGLVGEGKMWSPKSGWADAKYVLEAHGLKPVILKPK
EGLALINGTQMITSLGCEAVERASAIARQADIVAALTLEVLKGTTKAFDTDIHALRPHRG
QIEVAFRFRSLLDSDHHPSEIAESHRFCDRVQDAYTLRCCPQVHGVVNDTIAFVKNIITT
ELNSATDNPMVFANRGETVSGGNFHGEYPAKALDYLAIGIHELAAISERRIERLCNPSLS
ELPAFLVAEGGLNSGFMIAHCTAAALVSENKALCHPSSVDSLSTSAATEDHVSMGGWAAR
KALRVIEHVEQVLAIELLAACQGIEFLRPLKTTTPLEKVYDLVRSVVRPWIKDRFMAPDI
EAAHRLLLEQKVWEVAAPYIEKYRMEHIPESRPLSPTAFSLQFLHKKSTKIPESEDL
Enzyme 6 Number of Residues 657
Enzyme 6 Molecular Weight 72698
Enzyme 6 Theoretical pI 6.95
Enzyme 6 GO Classification
Function
  • acid-ammonia (or amide) ligase activity
  • ammonia ligase activity
  • ammonia-lyase activity
  • carbon-nitrogen lyase activity
  • catalytic activity
  • histidine ammonia-lyase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • lyase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • biosynthesis
  • cellular metabolism
  • histidine catabolism
  • histidine family amino acid metabolism
  • histidine metabolism
  • metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 6 General Function Amino acid transport and metabolism
Enzyme 6 Specific Function L-histidine = urocanate + NH(3)
Enzyme 6 Pathways
Enzyme 6 Reactions
  • L-histidine = urocanate + NH3
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 451210 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P42357 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name HUTH_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1974 bp 
ATGCCCAGATACACGGTGCACGTACGTGGGGAATGGCTGGCAGTGCCCTGCCAGGACGCG
CAGCTCACTGTGGGCTGGCTGGGCCGGGAGGCCGTGAGGCGCTATATCAAGAATAAGCCC
GACAATGGTGGCTTCACCTCCGTGGATGACGCGCACTTCCTTGTGCGCCGGTGCAAGGGC
CTGGGCCTGCTGGACAACGAGGACCGGCTCGAGGTGGCCCTAGAGAACAACGAGTTCGTG
GAAGTGGTTATAGAGGGTGATGCCATGTCTCCTGACTTCATTCCATCTCAACCAGAAGGA
GTTTATCTATACAGCAAGTACCGGGAGCCTGAAAAGTACATCGAGTTAGATGGAGACCGT
CTGACCACGGAGGATCTGGTCAACTTGGGAAAGGGACGCTACAAAATAAAGCTCACCCCA
ACAGCTGAGAAGAGGGTGCAGAAATCCAGGGAGGTCATAGATAGCATCATAAAAGAGAAA
ACAGTTGTTTACGGTATTACTACAGGTTTTGGGAAATTTGCCAGAACTGTAATTCCTATC
AATAAGCTACAGGAGCTTCAGGTCAACTTAGTACGCTCACATTCTTCAGGTGTTGGGAAA
CCACTAAGTCCTGAGAGGTGTCGGATGCTCTTGGCTTTAAGGATCAATGTCTTAGCCAAA
GGATACAGTGGCATTTCCCTGGAGACCCTCAAACAAGTCATAGAAATGTTTAATGCCTCC
TGCCTGCCCTATGTCCCAGAGAAAGGAACCGTTGGTGCCAGTGGAGACCTTGCCCCACTC
TCTCATCTTGCTCTTGGGCTAGTTGGAGAAGGGAAGATGTGGTCTCCGAAGAGTGGCTGG
GCTGATGCTAAATACGTGCTAGAAGCCCATGGATTGAAACCAGTTATTTTAAAACCAAAA
GAGGGCCTGGCACTCATCAATGGGACGCAGATGATCACATCCCTGGGCTGTGAAGCTGTA
GAGCGAGCCAGTGCTATTGCACGGCAGGCTGACATTGTGGCAGCCCTGACCCTTGAGGTG
CTGAAGGGCACCACCAAAGCCTTTGACACTGACATTCATGCTCTTCGACCTCACCGTGGG
CAAATTGAAGTTGCTTTTCGGTTTCGGTCACTCTTGGACTCAGATCACCACCCATCAGAA
ATAGCAGAGAGTCACAGGTTCTGTGATCGCGTCCAGGATGCATACACCTTGCGCTGCTGT
CCACAGGTCCATGGTGTGGTGAATGATACAATAGCATTTGTGAAGAACATCATTACCACA
GAACTGAACAGCGCAACAGATAATCCTATGGTCTTTGCCAATAGGGGAGAGACAGTTTCT
GGAGGAAACTTCCATGGTGAATACCCAGCCAAAGCCCTAGACTACTTGGCCATTGGCATC
CATGAACTTGCTGCAATCAGTGAGAGAAGAATCGAGCGGCTCTGCAATCCCTCCCTCAGT
GAGCTGCCTGCCTTCCTGGTGGCTGAAGGTGGTCTGAACTCTGGGTTCATGATAGCTCAC
TGCACGGCAGCAGCCCTTGTTTCTGAGAACAAGGCTCTGTGCCATCCCTCGTCTGTTGAC
TCCCTCTCCACCAGCGCAGCCACGGAGGACCACGTCTCCATGGGAGGATGGGCAGCAAGG
AAAGCCCTCAGGGTCATCGAGCATGTGGAGCAAGTGCTGGCCATCGAGCTCCTTGCAGCC
TGCCAGGGCATAGAGTTTCTACGTCCCCTGAAAACAACCACTCCGCTGGAGAAGGTCTAT
GACCTGGTGCGCTCTGTTGTAAGGCCCTGGATAAAAGATCGCTTCATGGCCCCGGACATC
GAGGCAGCCCACAGGCTGCTCCTGGAGCAGAAGGTTTGGGAAGTAGCTGCTCCATACATT
GAAAAATACAGAATGGAGCATATTCCAGAATCAAGACCTCTTTCTCCAACAGCCTTTTCA
CTGCAATTTCTGCACAAGAAATCCACCAAAATCCCGGAGTCTGAGGACCTTTAA
Enzyme 6 GenBank Gene ID D16626 Link Image
Enzyme 6 GeneCard ID HAL Link Image
Enzyme 6 GenAtlas ID HAL Link Image
Enzyme 6 HGNC ID HGNC:4806 Link Image
Enzyme 6 Chromosome Location 12
Enzyme 6 Locus 12q22-q24.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Suchi M, Harada N, Wada Y, Takagi Y: Molecular cloning of a cDNA encoding human histidase. Biochim Biophys Acta. 1993 Nov 16;1216(2):293-5. [PubMed Link Image]
  2. Suchi M, Sano H, Mizuno H, Wada Y: Molecular cloning and structural characterization of the human histidase gene (HAL). Genomics. 1995 Sep 1;29(1):98-104. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 6167
Enzyme 7 Name Histidine decarboxylase
Enzyme 7 Synonyms
  1. HDC
Enzyme 7 Gene Name HDC
Enzyme 7 Protein Sequence >Histidine decarboxylase 
MMEPEEYRERGREMVDYICQYLSTVRERRVTPDVQPGYLRAQLPESAPEDPDSWDSIFGD
IERIIMPGVVHWQSPHMHAYYPALTSWPSLLGDMLADAINCLGFTWASSPACTELEMNVM
DWLAKMLGLPEHFLHHHPSSQGGGVLQSTVSESTLIALLAARKNKILEMKTSEPDADESC
LNARLVAYASDQAHSSVEKAGLISLVKMKFLPVDDNFSLRGEALQKAIEEDKQRGLVPVF
VCATLGTTGVCAFDCLSELGPICAREGLWLHIDAAYAGTAFLCPEFRGFLKGIEYADSFT
FNPSKWMMVHFDCTGFWVKDKYKLQQTFSVNPIYLRHANSGVATDFMHWQIPLSRRFRSV
KLWFVIRSFGVKNLQAHVRHGTEMAKYFESLVRNDPSFEIPAKRHLGLVVFRLKGPNCLT
ENVLKEIAKAGRLFLIPATIQDKLIIRFTVTSQFTTRDDILRDWNLIRDAATLILSQHCT
SQPSPRVGNLISQIRGARAWACGTSLQSVSGAGDDPVQARKIIKQPQRVGAGPMKRENGL
HLETLLDPVDDCFSEEAPDATKHKLSSFLFSYLSVQTKKKTVRSLSCNSVPVSAQKPLPT
EASVKNGGSSRVRIFSRFPEDMMMLKKSAFKKLIKFYSVPSFPECSSQCGLQLPCCPLQA
MV
Enzyme 7 Number of Residues 662
Enzyme 7 Molecular Weight 74141
Enzyme 7 Theoretical pI 8.06
Enzyme 7 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 7 General Function Amino acid transport and metabolism
Enzyme 7 Specific Function L-histidine = histamine + CO(2)
Enzyme 7 Pathways
Enzyme 7 Reactions
  • L-histidine = histamine + CO2
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 32109 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P19113 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name DCHS_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1989 bp 
ATGATGGAGCCTGAGGAGTACAGAGAGAGAGGGAGAGAGATGGTGGATTACATCTGCCAG
TACCTGAGCACTGTGCGGGAGAGACGTGTGACGCCAGACGTGCAGCCTGGCTACCTGCGA
GCCCAGCTGCCTGAGAGTGCTCCTGAGGACCCCGACAGCTGGGACAGCATCTTTGGGGAC
ATTGAACGAATCATCATGCCTGGGGTGGTACATTGGCAGAGCCCCCATATGCACGCCTAC
TACCCAGCCCTCACCTCTTGGCCCTCCCTGCTAGGAGACATGCTGGCTGATGCCATCAAC
TGCTTGGGATTCACCTGGGCATCCAGCCCTGCGTGTACAGAGCTGGAGATGAACGTCATG
GACTGGTTGGCAAAAATGCTGGGACTTCCAGAGCACTTCTTGCACCACCACCCCAGCAGC
CAGGGCGGAGGCGTCCTGCAGCAGACGGTCAGTGAATCCACTTTGATTGCCCTGCTGGCA
GCAAGGAAGAACAAAATCCTGGAAATGAAAACGTCTGAGCCCGATGCTGATGAGTCCTGC
CTAAATGCCCGACTCGTGGCCTATGCCTCTGACCAGGCTCACTCCTCTGTGGAAAAGGCT
GGTTTGATTTCCCTTGTGAAGATGAAATTTCTGCCTGTGGATGACAACTTCTCACTCCGA
GGGGAAGCTCTTCAGAAGGCCATCGAGGAAGACAAGCAGCGGGGCTTGGTGCCCGTCTTT
GTCTGTGCAACACTAGGGACCACTGGGGTCTGTGCATTTGACTGCCTGTCAGAGCTGGGC
CCCATCTGTGCCCGTGAGGGGCTGTGGCTCCACATCGATGCTGCTTATGCAGGCACTGCC
TTCCTGTGCCCCGAGTTCCGGGGGTTTCTGAAGGGGATTGAGTATGCCGACTCCTTCACC
TTTAATCCTTCCAAGTGGATGATGGTGCATTTTGACTGTACTGGGTTCTGGGTCAAGGAC
AAGTACAAGCTGCAGCAGACCTTCAGTGTGAATCCCATCTACCTCAGGCATGCCAACTCA
GGCGTGGCCACCGACTTCATGCACTGGCAGATCCCCCTGAGCCGACGGTTTCGCTCTGTT
AAACTCTGGTTCGTGATTCGGTCCTTCGGGGTGAAGAATCTTCAAGCACATGTCAGACAT
GGTACTGAAATGGCTAAATATTTTGAATCTCTGGTCAGAAACGACCCTTCCTTTGAAATT
CCTGCCAAGAGGCACCTTGGCCTGGTGGTTTTTCGTCTAAAGGGTCCTAATTGTCTCACA
GAAAATGTGTTAAAGGAAATAGCTAAAGCTGGCCGTCTCTTCCTCATCCCGGCCACTATC
CAGGACAAGTTAATCATCCGTTTCACTGTGACATCCCAGTTTACCACTAGGGATGACATC
CTGAGAGACTGGAATCTCATTCGAGATGCTGCCACTCTCATCCTGAGTCAGCACTGTACT
TCCCAACCCAGCCCTCGGGTTGGGAACCTCATCTCCCAAATCAGGGGTGCCAGAGCCTGG
GCCTGTGGAACGTCCCTTCAGTCTGTCAGTGGGGCAGGAGATGATCCAGTCCAGGCCAGG
AAGATCATCAAGCAGCCTCAGCGTGTGGGAGCCGGTCCCATGAAAAGGGAAAATGGCCTC
CATCTTGAAACCCTGCTGGACCCAGTTGATGACTGCTTTTCAGAAGAGGCCCCAGATGCC
ACCAAGCACAAGCTGTCCTCCTTCCTGTTCAGTTACTTGTCTGTGCAGACTAAGAAGAAG
ACGGTGCGCTCCCTCAGTTGCAACAGTGTGCCAGTGAGTGCTCAGAAGCCACTGCCCACA
GAGGCCTCTGTGAAGAATGGGGGCTCCTCCAGGGTCAGAATCTTTTCCAGGTTTCCAGAA
GACATGATGATGCTGAAGAAAAGTGCCTTCAAAAAACTCATCAAATTCTACAGCGTCCCC
AGCTTTCCTGAATGCAGCTCTCAATGTGGACTCCAGCTGCCCTGTTGCCCTCTGCAGGCC
ATGGTTTAG
Enzyme 7 GenBank Gene ID X54297 Link Image
Enzyme 7 GeneCard ID HDC Link Image
Enzyme 7 GenAtlas ID HDC Link Image
Enzyme 7 HGNC ID HGNC:4855 Link Image
Enzyme 7 Chromosome Location 15
Enzyme 7 Locus 15q21-q22
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Yamauchi K, Sato R, Tanno Y, Ohkawara Y, Maeyama K, Watanabe T, Satoh K, Yoshizawa M, Shibahara S, Takishima T: Nucleotide sequence of the cDNA encoding L-histidine decarboxylase derived from human basophilic leukemia cell line, KU-812-F. Nucleic Acids Res. 1990 Oct 11;18(19):5891. [PubMed Link Image]
  2. Zahnow CA, Yi HF, McBride OW, Joseph DR: Cloning of the cDNA encoding human histidine decarboxylase from an erythroleukemia cell line and mapping of the gene locus to chromosome 15. DNA Seq. 1991;1(6):395-400. [PubMed Link Image]
  3. Mamune-Sato R, Yamauchi K, Tanno Y, Ohkawara Y, Ohtsu H, Katayose D, Maeyama K, Watanabe T, Shibahara S, Takishima T: Functional analysis of alternatively spliced transcripts of the human histidine decarboxylase gene and its expression in human tissues and basophilic leukemia cells. Eur J Biochem. 1992 Oct 15;209(2):533-9. [PubMed Link Image]
  4. Yatsunami K, Ohtsu H, Tsuchikawa M, Higuchi T, Ishibashi K, Shida A, Shima Y, Nakagawa S, Yamauchi K, Yamamoto M, et al.: Structure of the L-histidine decarboxylase gene. J Biol Chem. 1994 Jan 14;269(2):1554-9. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 8562
Enzyme 8 Name System N amino acid transporter 1
Enzyme 8 Synonyms
  1. SN1
  2. N-system amino acid transporter 1
  3. Solute carrier family 38 member 3
Enzyme 8 Gene Name SLC38A3
Enzyme 8 Protein Sequence >System N amino acid transporter 1 
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
Enzyme 8 Number of Residues 504
Enzyme 8 Molecular Weight 55774
Enzyme 8 Theoretical pI 8.01
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Amino acid transport and metabolism
Enzyme 8 Specific Function Sodium-dependent amino acid/proton antiporter. Mediates electrogenic cotransport of glutamine and sodium ions in exchange for protons. Also recognizes histidine, asparagine and alanine. May mediate amino acid transport in either direction under physiological conditions. May play a role in nitrogen metabolism and synaptic transmission
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-111
Enzyme 8 Transmembrane Regions
  • 83-103 106-126 144-164 187-207 213-233 324-344 366-386 408-428 431-451 471-491
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID Q99624 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name S38A3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AF244548 Link Image
Enzyme 8 GeneCard ID SLC38A3 Link Image
Enzyme 8 GenAtlas ID SLC38A3 Link Image
Enzyme 8 HGNC ID HGNC:18044 Link Image
Enzyme 8 Chromosome Location 3
Enzyme 8 Locus 3p21.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Fei YJ, Sugawara M, Nakanishi T, Huang W, Wang H, Prasad PD, Leibach FH, Ganapathy V: Primary structure, genomic organization, and functional and electrogenic characteristics of human system N 1, a Na+- and H+-coupled glutamine transporter. J Biol Chem. 2000 Aug 4;275(31):23707-17. [PubMed Link Image]
  2. Lerman MI, Minna JD: The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium. Cancer Res. 2000 Nov 1;60(21):6116-33. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 17098
Enzyme 9 Name Solute carrier family 38, member 3, isoform CRA_b
Enzyme 9 Synonyms
  1. SubName: cDNA, FLJ94006, Homo sapiens solute carrier family 38, member 3 (SLC38A3), mRNA
Enzyme 9 Gene Name SLC38A3
Enzyme 9 Protein Sequence >Solute carrier family 38, member 3, isoform CRA_b 
MEAPLQTEMVELVPNGKHSEGLLPVITPMAGNQRVEDPARSCMEGKSFLQKSPSKEPHFT
DFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKS
SGVVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEE
KTSDWYMNGNYLVILVSVTIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFHVPC
PLPPNFNNTTGNFSHVEIVKEKVQLQVEPEASAFCTPSYFTLNSQTAYTIPIMAFAFVCH
PEVLPIYTELKDPSKKKMQHISNLSIAVMYIMYFLAALFGYLTFYNGVESELLHTYSKVD
PFDVLILCVRVAVLTAVTLTVPIVLFPVRRAIQQMLFPNQEFSWLRHVLIAVGLLTCINL
LVIFAPNILGIFGVIGATSAPFLIFIFPAIFYFRIMPTEKEPARSTPKILALCFAMLGFL
LMTMSLSFIIIDWASGTSRHGGNH
Enzyme 9 Number of Residues 504
Enzyme 9 Molecular Weight 55774
Enzyme 9 Theoretical pI 8.01
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Amino acid transport and metabolism
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID B2R8Q0 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B2R8Q0_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK313461 Link Image
Enzyme 9 GeneCard ID B2R8Q0 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available