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Human Metabolome Database Version 2.5

 

Showing metabocard for Citric acid (HMDB00094)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-28 10:45:17
Accession Number HMDB00094
Secondary Accession Numbers Not Available
Common Name Citric acid
Description Citric acid (citrate) is a weak acid that is formed in the tricarboxylic acid cycle or that may be introduced with diet. The evaluation of plasma citric acid is scarcely used in the diagnosis of human diseases. On the contrary urinary citrate excretion is a common tool in the differential diagnosis of kidney stones, renal tubular acidosis and it plays also a role in bone diseases. The importance of hypocitraturia should be considered with regard to bone mass, urine crystallization and urolithiasis. (PMID 12957820) The secretory epithelial cells of the prostate gland of humans and other animals posses a unique citrate-related metabolic pathway regulated by testosterone and prolactin. This specialized hormone-regulated metabolic activity is responsible for the major prostate function of the production and secretion of extraordinarily high levels of citrate. The key regulatory enzymes directly associated with citrate production in the prostate cells are mitochondrial aspartate aminotransferase, pyruvate dehydrogenase, and mitochondrial aconitase. testosterone and prolactin are involved in the regulation of the corresponding genes associated with these enzymes. The regulatory regions of these genes contain the necessary response elements that confer the ability of both hormones to control gene transcription. Protein kinase c (PKC) is the signaling pathway for the prolactin regulation of the metabolic genes in prostate cells. testosterone and prolactin regulation of these metabolic genes (which are constitutively expressed in all mammalian cells) is specific for these citrate-producing cells. (PMID 12198595) Citric acid is found in citrus fruits, most concentrated in lemons and limes, where it can comprise as much as 8% of the dry weight of the fruit. Citric acid is a natural preservative and is also used to add an acidic (sour) taste to foods and soft drinks. The salts of citric acid (citrates) can be used as anticoagulants due to their calcium chelating ability. Intolerance to citric acid in the diet is known to exist. Little information is available as the condition appears to be rare, but like other types of food intolerance it is often described as a "pseudo-allergic" reaction.
Synonyms
  1. 2-Hydroxy-1,2,3-propanetricarboxylate
  2. 2-Hydroxy-1,2,3-propanetricarboxylic acid
  3. 3-Carboxy-3-hydroxypentane-1,5-dioate
  4. 3-Carboxy-3-hydroxypentane-1,5-dioic acid
  5. Aciletten
  6. Anhydrous citrate
  7. Anhydrous citric acid
  8. Chemfill
  9. Citraclean
  10. Citrate
  11. Citretten
  12. Citric acid
  13. Citro
  14. E 330
  15. Hydrocerol A
  16. Kyselina citronova
  17. Suby G
  18. Uro-trainer
  19. beta-Hydroxytricarballylate
  20. beta-Hydroxytricarballylic acid
Chemical IUPAC Name 2-hydroxypropane-1,2,3-tricarboxylic acid
Chemical Formula C6H8O7
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Tricarboxylic Acids
Sub Class
  • Short chain tricarboxylic acids
Family
  • Mammalian Metabolite
Species
  • tertiary alcohol
  • carboxylic acid
  • alpha-hydroxyacid
Biofunction
  • Component of Glyoxylate and dicarboxylate metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 192.124
Monoisotopic Molecular Weight 192.027008
Isomeric SMILES OC(=O)CC(O)(CC(O)=O)C(O)=O
Canonical SMILES OC(=O)CC(O)(CC(O)=O)C(O)=O
KEGG Compound ID C00158 Link Image
BioCyc ID CIT Link Image
BiGG ID 34080 Link Image
Wikipedia Link Citric acid Link Image
NuGOwiki Link HMDB00094 Link Image
Metagene Link HMDB00094 Link Image
METLIN ID 124 Link Image
PubChem Compound 311 Link Image
PubChem Substance 10317680 Link Image
ChEBI ID 16947 Link Image
CAS Registry Number 77-92-9
InChI Identifier InChI=1/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12)
Synthesis Reference Evans, D. W. S. Hydrolysis of ethyl methylenecitrate [5,5-bis(ethoxycarbonylmethyl)-1,3-dioxolan-4-one] and an attempted synthesis of agaric acid. Journal of the Chemical Society (1959), 1313-14.
Melting Point (Experimental) 153 oC
Experimental Water Solubility 592.0 mg/mL [MERCK INDEX (1989)] Source: PhysProp
Predicted Water Solubility 105.99999 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity -1.64 [AVDEEF,A (1997)] Source: PhysProp
Predicted LogP/Hydrophobicity -1.33 [Predicted by ALOGPS]; -2.2 [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 1A59 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)
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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
  • mitochondria
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Blood
Value 88.0 +/- 33.0 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 Blood
Value 122.0 +/- 30.0 uM
Age Children:1-13 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 Blood
Value 190.0 (30.0-400.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid Blood
Value 54.2 +/- 0.8 uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Hoppe B, Kemper MJ, Hvizd MG, Sailer DE, Langman CB: Simultaneous determination of oxalate, citrate and sulfate in children's plasma with ion chromatography. Kidney Int. 1998 May;53(5):1348-52. [PubMed Link Image]
Biofluid CSF
Value 176.0 +/- 50.0 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 370.0 (110.0 - 630.0) 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 400.0 +/- 170.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Commodari F, Arnold DL, Sanctuary BC, Shoubridge EA: 1H NMR characterization of normal human cerebrospinal fluid and the detection of methylmalonic acid in a vitamin B12 deficient patient. NMR Biomed. 1991 Aug;4(4):192-200. [PubMed Link Image]
Biofluid CSF
Value 350.0 +/- 240.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid CSF
Value 225 +/- 96 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 Urine
Value 226.32 +/- 98.12 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 300.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Bairaktari E, Katopodis K, Siamopoulos KC, Tsolas O: Paraquat-induced renal injury studied by 1H nuclear magnetic resonance spectroscopy of urine. Clin Chem. 1998 Jun;44(6 Pt 1):1256-61. [PubMed Link Image]
Biofluid Urine
Value 172.8 +/- 87.4 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Psihogios NG, Gazi IF, Elisaf MS, Seferiadis KI, Bairaktari ET: Gender-related and age-related urinalysis of healthy subjects by NMR-based metabonomics. NMR Biomed. 2008 Mar;21(3):195-207. [PubMed Link Image]
Biofluid Urine
Value 280.6 +/- 115.2 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Psihogios NG, Gazi IF, Elisaf MS, Seferiadis KI, Bairaktari ET: Gender-related and age-related urinalysis of healthy subjects by NMR-based metabonomics. NMR Biomed. 2008 Mar;21(3):195-207. [PubMed Link Image]
Biofluid Urine
Value 972.5 (89.5-1647.7) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 708.9 (25.2-3168.4) umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 208.6 (33.2-445.1) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 184.2 (58.7-651.7) umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 181.0 +/- 97.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 242.0 +/- 129.6 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 1570 +/- 574 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
Concentrations (Abnormal)
Biofluid Blood
Value 141.3 +/- 54.7 uM
Age Adult:>18 yrs old
Sex Both
Condition Hyperoxalemia
Comments Before 4-hour dialysis session
References
  • Ogawa Y, Machida N, Jahana M, Gakiya M, Chinen Y, Oda M, Morozumi M, Sugaya K: Major factors modulating the serum oxalic acid level in hemodialysis patients. Front Biosci. 2004 Sep 1;9:2901-8. [PubMed Link Image]
Biofluid Blood
Value 117.6 +/- 37.2 uM
Age Adult:>18 yrs old
Sex Both
Condition Hyperoxalemia
Comments After 4-hour dialysis session
References
  • Ogawa Y, Machida N, Jahana M, Gakiya M, Chinen Y, Oda M, Morozumi M, Sugaya K: Major factors modulating the serum oxalic acid level in hemodialysis patients. Front Biosci. 2004 Sep 1;9:2901-8. [PubMed Link Image]
Biofluid CSF
Value 2400.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Canavan disease
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 Urine
Value 11.2 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Paraquat poisoning
Comments Not Available
References
  • Bairaktari E, Katopodis K, Siamopoulos KC, Tsolas O: Paraquat-induced renal injury studied by 1H nuclear magnetic resonance spectroscopy of urine. Clin Chem. 1998 Jun;44(6 Pt 1):1256-61. [PubMed Link Image]
Biofluid Urine
Value 268.0 (53.0-1111.0) umol/mmol creatinine
Age N/A
Sex Both
Condition Lung Cancer
Comments Not Available
References
  • HMP experiment
Biofluid Urine
Value 154 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Condition Rhabdomyolysis
Comments Not Available
References
  • Bairaktari E, Seferiadis K, Liamis G, Psihogios N, Tsolas O, Elisaf M: Rhabdomyolysis-related renal tubular damage studied by proton nuclear magnetic resonance spectroscopy of urine. Clin Chem. 2002 Jul;48(7):1106-9. [PubMed Link Image]
Associated Disorders
Condition References
Canavan disease
  • 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]
Hyperoxalemia
  • Ogawa Y, Machida N, Jahana M, Gakiya M, Chinen Y, Oda M, Morozumi M, Sugaya K: Major factors modulating the serum oxalic acid level in hemodialysis patients. Front Biosci. 2004 Sep 1;9:2901-8. [PubMed Link Image]
Lung Cancer
  • HMP experiment
Paraquat poisoning
  • Bairaktari E, Katopodis K, Siamopoulos KC, Tsolas O: Paraquat-induced renal injury studied by 1H nuclear magnetic resonance spectroscopy of urine. Clin Chem. 1998 Jun;44(6 Pt 1):1256-61. [PubMed Link Image]
Rhabdomyolysis
  • Bairaktari E, Seferiadis K, Liamis G, Psihogios N, Tsolas O, Elisaf M: Rhabdomyolysis-related renal tubular damage studied by proton nuclear magnetic resonance spectroscopy of urine. Clin Chem. 2002 Jul;48(7):1106-9. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Citric Acid Cycle SMP00057 Link Image map00020 Link Image
Transfer of Acetyl Groups into Mitochondria SMP00466 Link Image
General References
  1. Moreno AJ, Brown JM, Salinas JA, Feaster BL 3rd, Brown TJ: Ga-67 positivity in sarcoidosis of the skin with coincident thyroid uptake of uncertain etiology. Clin Nucl Med. 1984 Mar;9(3):165-6. [PubMed Link Image]
  2. Wenk J, Foitzik A, Achterberg V, Sabiwalsky A, Dissemond J, Meewes C, Reitz A, Brenneisen P, Wlaschek M, Meyer-Ingold W, Scharffetter-Kochanek K: Selective pick-up of increased iron by deferoxamine-coupled cellulose abrogates the iron-driven induction of matrix-degrading metalloproteinase 1 and lipid peroxidation in human dermal fibroblasts in vitro: a new dressing concept. J Invest Dermatol. 2001 Jun;116(6):833-9. [PubMed Link Image]
  3. Wei R, Han JJ, Bai B, Ren DL, Chen B, Yang MF, Xia ZL: Analysis of factors influencing the blood levels and activities of tissue-type plasminogen activator (t-PA). Clin Hemorheol Microcirc. 2003;29(3-4):351-6. [PubMed Link Image]
  4. McBane RD 2nd, Karnicki K, Tahirkheli N, Miller RS, Owen WG: Platelet characteristics associated with coronary artery disease. J Thromb Haemost. 2003 Jun;1(6):1296-303. [PubMed Link Image]
  5. Jurasovic J, Cvitkovic P, Pizent A, Colak B, Telisman S: Semen quality and reproductive endocrine function with regard to blood cadmium in Croatian male subjects. Biometals. 2004 Dec;17(6):735-43. [PubMed Link Image]
  6. Mairiang E, Hanpanich P, Sriboonlue P: In vivo 31P-MRS assessment of muscle-pH, cytolsolic-[Mg2+] and phosphorylation potential after supplementing hypokaliuric renal stone patients with potassium and magnesium salts. Magn Reson Imaging. 2004 Jun;22(5):715-9. [PubMed Link Image]
  7. Tammen H, Schulte I, Hess R, Menzel C, Kellmann M, Mohring T, Schulz-Knappe P: Peptidomic analysis of human blood specimens: comparison between plasma specimens and serum by differential peptide display. Proteomics. 2005 Aug;5(13):3414-22. [PubMed Link Image]
  8. Chiueh CC, Andoh T, Lai AR, Lai E, Krishna G: Neuroprotective strategies in Parkinson's disease: protection against progressive nigral damage induced by free radicals. Neurotox Res. 2000 May;2(2-3):293-310. [PubMed Link Image]
  9. Batchelor WB, Tolleson TR, Huang Y, Larsen RL, Mantell RM, Dillard P, Davidian M, Zhang D, Cantor WJ, Sketch MH Jr, Ohman EM, Zidar JP, Gretler D, DiBattiste PM, Tcheng JE, Califf RM, Harrington RA: Randomized COMparison of platelet inhibition with abciximab, tiRofiban and eptifibatide during percutaneous coronary intervention in acute coronary syndromes: the COMPARE trial. Comparison Of Measurements of Platelet aggregation with Aggrastat, Reopro, and Eptifibatide. Circulation. 2002 Sep 17;106(12):1470-6. [PubMed Link Image]
  10. A J, Trygg J, Gullberg J, Johansson AI, Jonsson P, Antti H, Marklund SL, Moritz T: Extraction and GC/MS analysis of the human blood plasma metabolome. Anal Chem. 2005 Dec 15;77(24):8086-94. [PubMed Link Image]
  11. Bairaktari E, Katopodis K, Siamopoulos KC, Tsolas O: Paraquat-induced renal injury studied by 1H nuclear magnetic resonance spectroscopy of urine. Clin Chem. 1998 Jun;44(6 Pt 1):1256-61. [PubMed Link Image]
  12. Wan KW, Malgesini B, Verpilio I, Ferruti P, Griffiths PC, Paul A, Hann AC, Duncan R: Poly(amidoamine) salt form: effect on pH-dependent membrane activity and polymer conformation in solution. Biomacromolecules. 2004 May-Jun;5(3):1102-9. [PubMed Link Image]
  13. Solheim BG, Flesland O, Brosstad F, Mollnes TE, Seghatchian J: Improved preservation of coagulation factors after pre-storage leukocyte depletion of whole blood. Transfus Apher Sci. 2003 Oct;29(2):133-9. [PubMed Link Image]
  14. Seiffert D, Thomas BE, Bradley JD, Munzer DA, Tchinnes MA, Kornhauser DM, Cain VA, Hua TA, Feuerstein GZ, Martin DE, Stern AM: Effects of the glycoprotein IIb/IIIa antagonist Roxifiban on P-selectin expression, fibrinogen binding, and microaggregate formation in a phase I dose-finding study: no evidence for platelet activation during treatment with a glycoprotein IIb/IIIa antagonist. Platelets. 2003 May;14(3):179-87. [PubMed Link Image]
  15. Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
  16. Odvina CV, Mason RP, Pak CY: Prevention of thiazide-induced hypokalemia without magnesium depletion by potassium-magnesium-citrate. Am J Ther. 2006 Mar-Apr;13(2):101-8. [PubMed Link Image]
  17. 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]
  18. Commodari F, Arnold DL, Sanctuary BC, Shoubridge EA: 1H NMR characterization of normal human cerebrospinal fluid and the detection of methylmalonic acid in a vitamin B12 deficient patient. NMR Biomed. 1991 Aug;4(4):192-200. [PubMed Link Image]
  19. McBane RD 2nd, Karnicki K, Miller RS, Owen WG: The impact of peripheral arterial disease on circulating platelets. Thromb Res. 2004;113(2):137-45. [PubMed Link Image]
  20. Abe T, Kobata H, Hanba Y, Kitabata Y, Narukawa N, Hasegawa H, Abe T, Fukagawa M: Study of plasma exchange for liver failure: beneficial and harmful effects. Ther Apher Dial. 2004 Jun;8(3):180-4. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. ATP-citrate synthase
  2. Citrate synthase, mitochondrial precursor
  3. Beta-Ala-His dipeptidase precursor
  4. Aconitate hydratase, mitochondrial precursor
  5. Iron-responsive element-binding protein 1
  6. Citrate lyase subunit beta-like protein, mitochondrial precursor
Enzyme 1 [top]
Enzyme 1 ID 5239
Enzyme 1 Name ATP-citrate synthase
Enzyme 1 Synonyms
  1. ATP-citrate
  2. pro-S--lyase
  3. Citrate cleavage enzyme
Enzyme 1 Gene Name ACLY
Enzyme 1 Protein Sequence >ATP-citrate synthase 
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
HRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG
IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRHPWDDISYVLPEHMSM
Enzyme 1 Number of Residues 1101
Enzyme 1 Molecular Weight 120841
Enzyme 1 Theoretical pI 7.34
Enzyme 1 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Energy production and conversion
Enzyme 1 Specific Function ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 28935 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P53396 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ACLY_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3318 bp 
ATGTCGGCCAAGGCAATTTCAGAGCAGACGGGCAAAGAACTCCTTTACAAGTTCATCTGT
ACCACCTCAGCCATCCAGAATCGGTTCAAGTATGCTCGGGTCACTCCTGACACAGACTGG
GCCCGCTTGCTGCAGGACCACCCCTGGCTGCTCAGCCAGAACTTGGTAGTCAAGCCAGAC
CAGCTGATCAAACGTCGTGGAAAACTTGGTCTCGTTGGGGTCGACCTCACTCTGGATGGG
GTCAAGTCCTGGCTGAAGCCACGGCTGGGACAGGAAGCCACAGTTGGCAAGGCCACAGGC
TTCCTCAAGAACTTTCTGATCGAGCCCTTCGCCCCCCACAGTCAGGCTGAGGAGTTCTAT
GTCTGCATCTATGCCACCCGAGAAGGGGACTACGTCCTGTTCCACCACGAGGGGGGTGTG
GACGTGGGTGATGTGGACGCCAAGGCCCAGAAGCTGCTTGTTGGCGTGGATGAGAAACTG
AATCCTGAGGACATCAAAAAACACCTGTTGGTCCACGCCCCTGACGACAAGAAAGAAATT
CTGGCCAGTTTTATCTCCGGCCTCTTCAATTTCTACGAGGACTTGTACTTCACCTACCTC
GAGATCAATCCCCTTGTAGTGACCAAAGATGGAGTCTATGTCCTTGACTTGGCGGCCAAG
GTGGACGCCACTGCCGACTACATCTGCAAAGTGAAGTGGGGTGACATCGAGTTCCCTCCC
CCCTTCGGGCGGGTGGCATATCCAGAGGAAGCCTACATTGCAGACCTCGATGCCAAAAGT
GGGGCAAGCCTGAAGCTGACCTTGCTGAACCCCAAAGGGAGGATCTGGACCATGGTGGCC
GGGGGTGGCGCCTCTGTCGTGTACAGCGATACCATCTGTGATCTAGGGGGTGTCAACGAG
CTGGCAAACTATGGGGAGTACTCAGGCGCCCCCAGCGAGCAGCAGACCTATGACTATGCC
AAGACTATCCTCTCCCTCATGACCCGAGAGAAGCACCCAGATGGCAAGATCCTCATCATT
GGAGGCAGCATCGCAAACTTCACCAACGTGGCTGCCACGTTCAAGGGCATCGTGAGAGCA
ATTCGAGATTACCAGGGCCCCCTGAAGGAGCACGAAGTCACAATCTTTGTCCGAAGAGGT
GGCCCCAACTATCAGGAGGGCTTACGGGTGATGGGAGAAGTCGGGAAGACCACTGGGATC
CCCATCCATGTCTTTGGCACAGAGACTCACATGACGGCCATTGTGGGCATGGCCTGGGCA
CCGGCCATCCCCAACCAGCCACCCACAGCGGCCCACACTGCAAACTTTCTCCTCAACGCC
CAGCGGGAGACATCGACTCCAGCCCCCAGCAGGACAGCATCTTTTTATGAGTCCATGGTC
GATGAGGTCAGGGCCGATGAGGTGGCGCCTGCAAAGAAGGCCAAGCCTGCCATGCCACAA
GATTCAGTCCCAAGTCCAAGATCCCTGCAAGGAAAGAGCACCACCCTCTTCAGCCGCCAC
ACCAAGGCCATTGTGTGGGGCATGCAGACCCGGGCCGTGCAAGGCATGCTGGACTTTGAC
TATGTCTGCTCCCGAGACGAGCCCTCAGTGGCTGCCATGGTCTATCCTTTCACTGGGGAC
CACAAGCAGAAGTTTTACTGGGGGCACAAAGAGATCCTGATCCCTGTCTTCAAGAACATG
GCTGATGCCATGAGGAAGCACCCGGAGGTAGATGTGCTCATCAACTTTGCCTCTCTCCGC
TCTGCCTATGACAGCACCATGGAGACCATGAACTATGCCCAGATCCGGACCATCGCCATC
ATAGCTGAAGGCATCCCTGAGGCCCTCACGAGAAAGCTGATCAAGAAGGCGGACCAGAAG
GGAGTGACCATCATCGGACCTGCCACTGTTGGAGGCATCAAGCCTGGGTGCTTTAAGATT
GGCAACACAGGTGGGATGCTGGACAACATCCTGGCCTCCAAACTGTACCCCCAGGCAGCT
GTGGCCTATGTCTCACGTTCCGGAGGCATGTCCAACGAGCTCAACAATATCATCTCTCGG
ACCACGGATGGCGTCTATGAGGGCGTGGCCATTGGTGGGGACAGGTACCCGGGCTCCACA
TTCATGGATCATGTGTTACGCTATCAGGACACTCCAGGAGTCAAAATGATTGTGGTTCTT
GGAGAGATTGGGGGCACTGAGGAATATAAGATTTCCCGGGGCATCAAGGAGGGCCGCCTC
ACTAAGCCCATCGTCTGCTGGTGCATCGGGACGTGTGCCACCATGTTCTCCTCTGAGGTC
CAGTTTGGCCATGCTGGAGCTTGTGCCAACCAGGCTTCTGAAACTGCAGTAGCCAAGAAC
CAGGCTTTGAAGGAAGCAGGAGTGTTTGTGCCCCGGAGCTTTGATGAGCTTGGAGAGATC
ATCCAGTCTGTATACGAAGATCTCGTGGCCAATGGAGTCATTGTACCTGCCCAGGAGGTG
CCGCCCCCAACCGTGCCCATGGACTACTCCTGGGCCAGGGAGCTTGGTTTGATCCGCAAA
CCTGCCTCGTTCATGACCAGCATCTGCGATGAGCGAGGACAGGAGCTCATCTACGCGGGC
ATGCCCATCACTGAGGTCTTCAAGGAAGAGATGGGCATTGGCGGGGCCCTCGGCCTCCTC
TGGTTCCAGAAAAGGTTGCCTAAGTACTCTTGCCAGTTCATTGAGATGTGTCTGATGGTG
ACAGCTGATCACGGGCCAGCCGTCTCTGGAGCCCACAACACCATCATTTGTGCGCGCACC
GCGGTGGAGCTGGTCTCCAGCCTCACCTCGGGGCTGCTCACCATCGGGGATCGGTTTGGG
GGTGCCTTGGATGCAGCAGCCAAGATGTTCAGTAAAGCCTTTGACAGTGGCATTATCCCC
ATGGAGTTTGTGAACAAGATGAAGAAGGAAGGGAAGCTGATCATGGGCATTGGTCACCGA
GTGAAGTCGATAAACAACCCAGACATGCGAGTGCAGATCCTCAAAGATTACGTCAGGCAG
CACTTCCCTGCCACTCCTCTGCTCGATTATGCACTGGAAGTAGAGAAGATTACCACCTCG
AAGAAGCCAAATCTTATCCTGAATGTAGATGGTCTCATCGGAGTCGCATTTGTAGACATG
CTTAGAAACTGTGGGTCCTTTACTCGGGAGGAAGCTGATGAATATATTGACATTGGAGCC
CTCAATGGCATCTTTGTGCTGGGAAGGAGTATGGGGTTCATTGGACACTATCTTGATCAG
AAGAGGCTGAAGCAGGGGCTGTATCGTCATCCGTGGGATGATATTTCATATGTTCTTCCG
GAACACATGAGCATGTAA
Enzyme 1 GenBank Gene ID X64330 Link Image
Enzyme 1 GeneCard ID ACLY Link Image
Enzyme 1 GenAtlas ID ACLY Link Image
Enzyme 1 HGNC ID HGNC:115 Link Image
Enzyme 1 Chromosome Location 17
Enzyme 1 Locus 17q12-q21
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS: Cloning and expression of a human ATP-citrate lyase cDNA. Eur J Biochem. 1992 Mar 1;204(2):491-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5272
Enzyme 2 Name Citrate synthase, mitochondrial precursor
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name CS
Enzyme 2 Protein Sequence >Citrate synthase, mitochondrial precursor 
MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVV
GQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLF
WLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESN
FARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNF
TNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPL
HGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQ
REFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYY
TVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
Enzyme 2 Number of Residues 466
Enzyme 2 Molecular Weight 51713
Enzyme 2 Theoretical pI 8.53
Enzyme 2 GO Classification
Function
  • catalytic activity
  • citrate (Si)-synthase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • main pathways of carbohydrate metabolism
  • metabolism
  • physiological process
  • tricarboxylic acid cycle
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Enzyme 2 Pathways
Enzyme 2 Reactions
  • acetyl-CoA + H2O + oxaloacetate = citrate + CoA
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-16
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 3288815 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O75390 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CISY_HUMAN Link Image
Enzyme 2 PDB ID 4CTS Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1401 bp 
ATGGCTTTACTTACTGCGGCCGCCCGGCTCTTGGGAACCAAGAATGCATCTTGTCTTGTT
CTTGCAGCCCGGCATGCTAGTGCTTCCTCCACGAATTTGAAAGACATATTGGCTGACCTG
ATACCTAAGGAGCAGGCCAGAATTAAGACTTTCAGGCAGCAACATGGCAAGACGGTGGTG
GGCCAAATCACTGTGGACATGATGTATGGTGGCATGAGAGGCATGAAGGGATTGGTGTAT
GAAACATCAGTTCTTGATCCTGATGAGGGCATCCGTTTCCGAGGCTTTAGTATCCCTGAA
TGCCAGAAACTGCTACCCAAGGCTAAGGGTGGGGAAGAACCCCTGCCTGAGGGCTTATTT
TGGCTGCTGGTAACTGGATGTATCCCAACAGAGGAACAGGTATCTTGGCTCTCAAAAGAG
TGGGCAAAGAGGGCAGCTCTGCCTTCCCATGTGGTCACCATGCTGGACAACTTTCCCACC
AATCTACACCCCATGTCTCAGCTGAGTGCAGCTGTTACAGCCCTCAACAGTGAAAGTAAC
TTTGCCCAAGCATATGCACGGGGTATCAGCCGAACCAAGTACTGGGAGTTGATTTATGAA
GATTCTGTGGATCTAATAGCAAAGCTACCTTGTGTTGCAGCAAAGATCTACCGAAATCTC
TACTGGGAAGGCAGCGGTATTGGGGCCATTGACTCTAACCTGGACTGGTCTCACAATTTC
ACCAACATGTTAGGCTATACTGATCATCAGTTCACTGAGCTCATGCGCCTGTACCTCACC
ATCCACAGTGACCATGAGGGTGGCAATGTAAGTGCCCATACCAGCCACTTGGTGGGCAGT
GCCCTTTCCGACCCTTACCTGTCCTTTGCAGCAGCCATGAACGGGCTGGCAGGGCCTCTC
CATGGACTGGCAAATCAGGAAGTGCTTGTCTGGCTAACACAGCTGCAGAAGGAAGTTGGC
AAAGATGTGTCAGATGAGAAGTTACGAGACTACATCTGGAACACACTCAACTCAGGACGG
GTTGTTCCAGGCTATGGCCATGCAGTACTAAGGAAGACTGATCCGCGATATACCTGTCAG
CGAGAGTTTGCTCTGAAACACCTGCCTAATGACCCCATGTTTAAGTTGGTTGCTCAGCTG
TACAAGATTGTGCCCAATGTCCTCTTAGAGCAGGGTAAAGCCAAGAATCCTTGGCCCAAT
GTAGATGCTCACAGTGGGGTGCTGCTCCAGTATTATGGCATGACGGAGATGAATTACTAC
ACGGTCCTGTTTGGGGTGTCACGAGCATTGGGTGTACTGGCACAGCTCATCTGGAGCCGA
GCCTTAGGCTTCCCTCTAGAAAGGCCCAAGTCCATGAGCACAGAGGGTCTGATGAAGTTT
GTGGACTCTAAGTCAGGGTAA
Enzyme 2 GenBank Gene ID AF047042 Link Image
Enzyme 2 GeneCard ID CS Link Image
Enzyme 2 GenAtlas ID CS Link Image
Enzyme 2 HGNC ID HGNC:2422 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12q13.2-q13.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Goldenthal MJ, Marin-Garcia J, Ananthakrishnan R: Cloning and molecular analysis of the human citrate synthase gene. Genome. 1998 Oct;41(5):733-8. [PubMed Link Image]
  2. Liu Q, Yu L, Han XF, Fu Q, Zhang JX, Tang H, Zhao SY: [Cloning and tissue expression pattern analysis of the human citrate synthase cDNA] Shi Yan Sheng Wu Xue Bao. 2000 Sep;33(3):207-14. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5713
Enzyme 3 Name Beta-Ala-His dipeptidase precursor
Enzyme 3 Synonyms
  1. Carnosine dipeptidase 1
  2. CNDP dipeptidase 1
  3. Serum carnosinase
  4. Glutamate carboxypeptidase-like protein 2
Enzyme 3 Gene Name CNDP1
Enzyme 3 Protein Sequence >Beta-Ala-His dipeptidase precursor 
MDPKLGRMAASLLAVLLLLLERGMFSSPSPPPALLEKVFQYIDLHQDEFVQTLKEWVAIE
SDSVQPVPRFRQELFRMMAVAADTLQRLGARVASVDMGPQQLPDGQSLPIPPVILAELGS
DPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAF
RALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAIT
YGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHILVPGIYDEVV
PLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFDEPG
TKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIA
NIDDTQYLAAKRAIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQ
NEKINRWNYIEGTKLFAAFFLEMAQLH
Enzyme 3 Number of Residues 507
Enzyme 3 Molecular Weight 56693
Enzyme 3 Theoretical pI 4.95
Enzyme 3 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 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine
Enzyme 3 Pathways
Enzyme 3 Reactions
  • Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-26
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 16555792 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q96KN2 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CNDP1_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 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 3 GenBank Gene ID AJ417564 Link Image
Enzyme 3 GeneCard ID CNDP1 Link Image
Enzyme 3 GenAtlas ID CNDP1 Link Image
Enzyme 3 HGNC ID HGNC:20675 Link Image
Enzyme 3 Chromosome Location 18
Enzyme 3 Locus 18q22.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6000
Enzyme 4 Name Aconitate hydratase, mitochondrial precursor
Enzyme 4 Synonyms
  1. Citrate hydro-lyase
  2. Aconitase
Enzyme 4 Gene Name ACO2
Enzyme 4 Protein Sequence >Aconitate hydratase, mitochondrial precursor 
MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLN
RPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAV
PSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILEN
YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSG
WSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYN
HRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHP
VAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGS
EQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRN
DANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPG
QDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAA
GPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVI
GDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHP
VDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ
Enzyme 4 Number of Residues 780
Enzyme 4 Molecular Weight 85426
Enzyme 4 Theoretical pI 7.65
Enzyme 4 GO Classification
Function
  • aconitate hydratase activity
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • cation binding
  • hydro-lyase activity
  • ion binding
  • iron ion binding
  • lyase activity
  • transition metal ion binding
Process
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • main pathways of carbohydrate metabolism
  • metabolism
  • physiological process
  • tricarboxylic acid cycle
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • mitochondrion
  • organelle
Enzyme 4 General Function Energy production and conversion
Enzyme 4 Specific Function Citrate = cis-aconitate + H(2)O
Enzyme 4 Pathways
Enzyme 4 Reactions
  • citrate = cis-aconitate + H2O
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 1718502 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q99798 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ACON_HUMAN Link Image
Enzyme 4 PDB ID 1B0J Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2343 bp 
ATGGCGCCCTACAGCCTACTGGTGACTCGGCTGCAGAAAGCTCTGGGTGTGCGGCAGTAC
CATGTGGCCTCAGTCCTGTGCCAACGGGCCAAGGTGGCGATGACGCATTTTGAGCCCAAC
GAGTACATCCATTATGACCTGCTAGAGAAGAACATTAACATTGTTCGCAAACGACTGAAC
CGGCCGCTGACACTCTCGGAGAAGATTGTGTATGGACACCTGGATGACCCCGCCAGCCAG
GAAATTGAGCGAGGCAAGTCGTACCTGCGGCTGCGGCCCGACCGTGTGGCCATGCAGGAT
GCGACGGCCCAGATGGCCATGCTCCAGTTCATCAGCAGCGGGCTGTCCAAGGTGGCTGTG
CCATCCACCATCCACTGTGACCATCTGATTGAAGCCCAGGTTGGGGACGAGAAAGACCTG
CGCCGGGCCAAGGACATCAACCAGGAAGTTTATAATTTCCTGGCAACTGCAGGTGACAAG
TATGGCGTGGGCTTCTGGAGCCCTGGATCTGGAATCATTCACCAGATTATTCTCGAAAAC
TATGCGTACCCTGGAGTTCTTCTGATTGGAACTGACTCCCACACCCCCAATGGTGGTGGC
CTAGGAGGCATCTGCATTGGAGTAGGGGGTGCAGATGCTGTGGATGTCATGGCTGGGATC
CCCTGGGAGCTGAAGTGCCCCAAGGTGATTGGCGTGAAGCTGACGGGCTCTCTCTCCGGT
TGGACCTCACCCAAAGATGTGATCCTGAAGGTGGCAGGCATCCTCACGGTGAAAGGTGGC
ACAGGTGCAATCGTGGAATACCACGGGCCTGGTGTAGACTCCATGTCCTGCACTGGCATG
GCGACAATCTGCAACATGGGTGCAGAAATTGGGGCCACCACTTCCGTGTTCCCTTACAAC
CACAGGATGAAGAAGTACCTGAGCAAGACCGGCCGGGAAGACATTGCCAATCTAGCTGAT
GAATTCAAGGATCACTTGGTGCCTGACCCTGGCTGCCATTATGACCAACTAATTGAAATT
AACCTCAGTGAGCTGAAGCCACACATCAATGGGCCCTTCACCCCTGACCTGGCTCACCCT
GTGGCAGAAGTGGGCAAGGTGGCAGAGAAGGAAGGATGGCCTCTGGACATCCGAGTGGGT
CTAATTGGTAGCTGCACCAATTCAAGCTATGAAGATATGGGGCGCTCAGCAGCTGTGGCC
AAGCAGGCACTGGCCCATGGACTCAAGTGCAAGTCCCAGTTCACCATCACTCCAGGTTCC
GAGCAGATCCGCGCCACCATTGAGCGGGACGGCTATGCACAGATCCTGAGGGATCTGGGT
GGCATTGTCCTGGCCAATGCCTGCGGGCCCTGCATTGGCCAGTGGGACAGAAAGGACATC
AAGAAGGGGGAGAAGAACACAATCGTCACCTCCTACAACAGGAACTTCACGGGCCGCAAC
GACGCAAACCCCGAGACCCATGCCTTTGTCACGTCCCCAGAGATTGTCACAGCCCTGGCC
ATTGCAGGAACCCTCAAGTTCAACCCAGAGACCGACTACCTGACAGGCAAGGATGGCAAG
AAGTTCAGGCTGGAAGCTCCGGATGCAGATGAGCTTCCCAAAGGGGAGTTTGACCCAGGG
CAGGACACCTACCAGCACCCCCCAAAGGACAGCAGCAGGCAGCATGTGGACGTGAGCCCC
ACCAGCCAGCGCCTGCAGCTCCTGGAGCCTTTTGACAAGTGGGATGGCAAGGACCTGGAG
GACCTGCAGATCCTCATCAAGGTCAAAGGGAAGTGTACCACTGACCACATCTCAGCTGCT
GGCCCCTGGCTCAAGTTCCGTGGGCACTTGGATAACATCTCCAACAACCTGCTCATTGGT
GCCATCAACATTGAAAACGGCAAGGCCAACTCCGTGCGCAATGCCGTCACTCAGGAGTTT
GGCCCCGTCCCTGACACTGCCCGCTACTACAAGAAACATGGCATCAGGTGGGTGGTGATC
GGAGACGAGAACTACGGCGAGGGCTCGAGCCGGGAGCATGCAGCTCTGGAGCCTCGCCAC
CTTGGGGGCCGGGCCATCATCACCAAGAGCTTTGCCAGGATCCACGAGACCAACCTGAAG
AAACAGGGCCTGCTGCCTCTGACCTTCGCTGACCCGGCTGACTACAACAAGATTCACCCT
GTGGACAAGCTGACCATTCAGGGCCTGAAGGACTTCACCCCTGGCAAGCCCCTGAAGTGC
ATCATCAAGCACCCCAACGGGACCCAGGAGACCATCCTCCTGAACCACACCTTCAACGAG
ACGCAGATTGAGTGGTTCCGCGCTGGCAGTGCCCTCAACAGAATGAAGGAACTGCAACAG
TGA
Enzyme 4 GenBank Gene ID U80040 Link Image
Enzyme 4 GeneCard ID ACO2 Link Image
Enzyme 4 GenAtlas ID ACO2 Link Image
Enzyme 4 HGNC ID HGNC:118 Link Image
Enzyme 4 Chromosome Location 22
Enzyme 4 Locus 22q11.2-q13.31|22q13.2-q13.31
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Mirel DB, Marder K, Graziano J, Freyer G, Zhao Q, Mayeux R, Wilhelmsen KC: Characterization of the human mitochondrial aconitase gene (ACO2). Gene. 1998 Jun 15;213(1-2):205-18. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6001
Enzyme 5 Name Iron-responsive element-binding protein 1
Enzyme 5 Synonyms
  1. IRE-BP 1
  2. Iron regulatory protein 1
  3. IRP1
  4. Ferritin repressor protein
  5. Aconitate hydratase
  6. Citrate hydro-lyase
  7. Aconitase
Enzyme 5 Gene Name ACO1
Enzyme 5 Protein Sequence >Iron-responsive element-binding protein 1 
MSNPFAHLAEPLDPVQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDI
ENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPA
DLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRIIPPGSGIIHQV
NLEYLARVVFDQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLP
QVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMC
PEYGATAAFFPVDEVSITYLVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQDPDFTQVVE
LDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKGFQVAPEHHNDHKTFIYDNT
EFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTY
YLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEG
RVHPNTRANYLASPPLVIAYAIAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVE
RQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPFFENLTLDLQPPK
SIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMA
RGTFANIRLLNRFLNKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSR
DWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTIIIP
ENLKPQMKVQVKLDTGKTFQAVMRFDTDVELTYFLNGGILNYMIRKMAK
Enzyme 5 Number of Residues 889
Enzyme 5 Molecular Weight 98400
Enzyme 5 Theoretical pI 6.66
Enzyme 5 GO Classification
Function
  • RNA binding
  • aconitate hydratase activity
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • cation binding
  • hydro-lyase activity
  • ion binding
  • iron ion binding
  • lyase activity
  • nucleic acid binding
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function This protein also expresses aconitase activity
Enzyme 5 Pathways
Enzyme 5 Reactions
  • citrate = cis-aconitate + H2O
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 33963 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P21399 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name IREB1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2670 bp 
ATGAGCAACCCATTCGCACACCTTGCTGAGCCATTGGATCCTGTACAACCAGGAAAGAAA
TTCTTCAATTTGAATAAATTGGAGGATTCAAGATATGGGCGCTTACCATTTTCGATCAGA
GTTCTTCTGGAAGCAGCCATTCGGAATTGTGATGAGTTTTTGGTGAAGAAACAGGATATT
GAAAATATTCTACATTGGAATGTCACTCAGCACAAGAACATAGAAGTGCCATTTAAGCCT
GCTCGTGTCATCCTGCAGGACTTTACGGGTGTGCCCGCTGTGGTTGACTTTGCTGCAATG
CGTGATGCTGTGAAAAAGTTAGGAGGAGATCCAGAGAAAATAAACCCTGTCTGCCCTGCT
GATCTTGTAATAGATCATTCCATCCAGGTTGATTTCAACAGAAGGGCAGACAGTTTACAG
AAGAATCAAGACCTGGAATTTGAAAGAAATAGAGAGCGATTTGAATTTTTAAAGTGGGGT
TCCCAGGCTTTTCACAACATGCGGATTATTCCCCCTGGCTCAGGAATCATCCACCAGGTG
AATTTGGAATATTTGGCAAGAGTGGTATTTGATCAGGATGGATATTATTACCCAGACAGC
CTCGTGGGCACAGACTCGCACACTACCATGATTGATGGCTTGGGCATTCTTGGTTGGGGT
GTCGGTGGTATTGAAGCAGAAGCTGTCATGCTGGGTCAGCCAATCAGTATGGTGCTTCCT
CAGGTGATTGGCTACAGGCTGATGGGGAAGCCCCACCCTCTGGTAACATCCACTGACATC
GTGCTCACCATTACCAAGCACCTCCGCCAGGTTGGGGTAGTGGGCAAATTTGTCGAGTTC
TTCGGGCCTGGAGTAGCCCAGTTGTCCATTGCTGACCGAGCTACGATTGCTAACATGTGT
CCAGAGTACGGAGCAACTGCTGCCTTTTTCCCAGTTGATGAAGTTAGTATCACGTACCTG
GTGCAAACAGGTCGTGATGAAGAAAAATTAAAGTATATTAAAAAATATCTTCAGGCTGTA
GGAATGTTTCGAGATTTCAATGACCCTTCTCAAGACCCAGACTTCACCCAGGTTGTGGAA
TTAGATTTGAAAACAGTAGTGCCTTGCTGTAGTGGACCCAAAAGGCCTCAGGACAAAGTT
GCTGTGTCCGACATGAAAAAGGACTTTGAGAGCTGCCTTGGAGCCAAGCAAGGATTTAAA
GGATTCCAAGTTGCTCCTGAACATCATAATGACCATAAGACCTTTATCTATGATAACACT
GAATTCACCCTTGCTCATGGTTCTGTGGTCATTGCTGCCATTACTAGCTGCACAAACACC
AGTAATCCGTCTGTGATGTTAGGGGCAGGATTGTTAGCAAAGAAAGCTGTGGATGCTGGC
CTGAACGTGATGCCTTACATCAAAACTAGCCTGTCTCCTGGGAGTGGCGTGGTCACCTAC
TACCTACAAGAAAGCGGAGTCATGCCTTATCTGTCTCAGCTTGGGTTTGACGTGGTGGGC
TATGGCTGCATGACCTGCATTGGCAACAGTGGGCCTTTACCTGAACCTGTGGTAGAAGCC
ATCACACAGGGAGACCTTGTAGCTGTTGGAGTACTATCTGGAAACAGGAATTTTGAAGGT
CGAGTTCACCCCAACACCCGGGCCAACTATTTAGCCTCTCCCCCCTTAGTAATAGCATAT
GCAATTGCTGGAACCATCAGAATCGACTTTGAGAAAGAGCCATTGGGAGTAAATGCAAAG
GGACAGCAGGTATTTCTGAAAGATATCTGGCCGACTAGAGACGAGATCCAGGCAGTGGAG
CGTCAGTATGTCATCCCGGGGATGTTTAAGGAAGTCTATCAGAAAATAGAGACTGTGAAT
GAAAGCTGGAATGCCTTAGCAACCCCATCAGATAAGCTGTTTTTCTGGAATTCCAAATCT
ACGTATATCAAATCACCACCATTCTTTGAAAACCTGACTTTGGATCTTCAGCCCCCTAAA
TCTATAGTGGATGCCTATGTGCTGCTAAATTTGGGAGATTCGGTAACAACTGACCACATC
TCCCCAGCTGGAAATATTGCAAGAAACAGTCCTGCTGCTCGCTACTTAACTAACAGAGGC
CTAACTCCACGAGAATTCAACTCCTATGGCTCCCGCCGAGGTAATGACGCCGTCATGGCA
CGGGGAACATTTGCCAACATTCGCTTGTTAAACAGATTTTTGAACAAGCAGGCACCACAG
ACTATCCATCTGCCTTCTGGGGAAATCCTTGATGTGTTTGATGCTGCTGAGCGGTACCAG
CAGGCAGGCCTTCCCCTGATCGTTCTGGCTGGCAAAGAGTACGGTGCAGGCAGCTCCCGA
GACTGGGCAGCTAAGGGCCCTTTCCTGCTGGGAATCAAAGCCGTCCTGGCCGAGAGCTAC
GAGCGCATTCACCGCAGTAACCTGGTTGGGATGGGTGTGATCCCACTTGAATATCTCCCT
GGTGAGAATGCAGATGCCCTGGGGCTCACAGGGCAAGAACGATACACTATCATTATTCCA
GAAAACCTCAAACCACAAATGAAAGTCCAGGTCAAGCTGGATACTGGCAAGACCTTCCAG
GCTGTCATGAGGTTTGACACTGATGTGGAGCTCACTTATTTCCTCAACGGGGGCATCCTC
AACTACATGATCCGCAAGATGGCCAAGTAG
Enzyme 5 GenBank Gene ID Z11559 Link Image
Enzyme 5 GeneCard ID ACO1 Link Image
Enzyme 5 GenAtlas ID ACO1 Link Image
Enzyme 5 HGNC ID HGNC:117 Link Image
Enzyme 5 Chromosome Location 9
Enzyme 5 Locus 9p22-q32|9p22-p13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Hirling H, Emery-Goodman A, Thompson N, Neupert B, Seiser C, Kuhn LC: Expression of active iron regulatory factor from a full-length human cDNA by in vitro transcription/translation. Nucleic Acids Res. 1992 Jan 11;20(1):33-9. [PubMed Link Image]
  2. Rouault TA, Tang CK, Kaptain S, Burgess WH, Haile DJ, Samaniego F, McBride OW, Harford JB, Klausner RD: Cloning of the cDNA encoding an RNA regulatory protein--the human iron-responsive element-binding protein. Proc Natl Acad Sci U S A. 1990 Oct;87(20):7958-62. [PubMed Link Image]
  3. Hentze MW, Argos P: Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase. Nucleic Acids Res. 1991 Apr 25;19(8):1739-40. [PubMed Link Image]
  4. Kaptain S, Downey WE, Tang C, Philpott C, Haile D, Orloff DG, Harford JB, Rouault TA, Klausner RD: A regulated RNA binding protein also possesses aconitase activity. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10109-13. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 11649
Enzyme 6 Name Citrate lyase subunit beta-like protein, mitochondrial precursor
Enzyme 6 Synonyms
  1. Citrate lyase beta-like
Enzyme 6 Gene Name CLYBL
Enzyme 6 Protein Sequence >Citrate lyase subunit beta-like protein, mitochondrial precursor 
MALRLLRRAARGAAAAALLRLKASLAADIPRLGYSSSSHHKYIPRRAVLYVPGNDEKKIK
KIPSLNVDCAVLDCEDGVAANKKNEARLRIVKTLEDIDLGPTEKCVRVNSVSSGLAEEDL
ETLLQSRVLPSSLMLPKVESPEEIQWFADKFSFHLKGRKLEQPMNLIPFVETAMGLLNFK
AVCEETLKVGPQVGLFLDAVVFGGEDFRASIGATSSKETLDILYARQKIVVIAKAFGLQA
IDLVYIDFRDGAGLLRQSREGAAMGFTGKQVIHPNQIAVVQEQFSPSPEKIKWAEELIAA
FKEHQQLGKGAFTFQGSMIDMPLLKQAQNTVTLATSIKEK
Enzyme 6 Number of Residues 340
Enzyme 6 Molecular Weight 37360
Enzyme 6 Theoretical pI Not Available
Enzyme 6 GO Classification
Function
  • carbon-carbon lyase activity
  • catalytic activity
  • citrate (pro-3S)-lyase activity
  • lyase activity
  • oxo-acid-lyase activity
Process
—
Component
  • citrate lyase complex
  • protein complex
Enzyme 6 General Function Carbohydrate transport and metabolism
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • Citrate --> Acetate + Oxaloacetate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 19073013 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q8N0X4 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name CLYBL_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence Not Available
Enzyme 6 GenBank Gene ID AF428253 Link Image
Enzyme 6 GeneCard ID Not Available
Enzyme 6 GenAtlas ID CLYBL Link Image
Enzyme 6 HGNC ID HGNC:18355 Link Image
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Morikawa J, Nishimura Y, Uchida A, Tanaka T: Molecular cloning of novel mouse and human putative citrate lyase beta-subunit. Biochem Biophys Res Commun. 2001 Dec 21;289(5):1282-6. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available