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Human Metabolome Database Version 2.5

 

Showing metabocard for Isocitric acid (HMDB00193)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-10 11:21:50
Accession Number HMDB00193
Secondary Accession Numbers Not Available
Common Name Isocitric acid
Description The citrate oxidation to isocitrate is catalyzed by the enzyme aconitase. Human prostatic secretion is remarkably rich in citric acid and low aconitase activity will therefore play a significant role in enabling accumulation of high citrate levels (PubMed ID 8115279)
Synonyms
  1. 1-Hydroxy-1,2,3-propanetricarboxylate
  2. 1-Hydroxy-1,2,3-propanetricarboxylic acid
  3. 1-Hydroxypropane-1,2,3-tricarboxylate
  4. 1-Hydroxypropane-1,2,3-tricarboxylic acid
  5. 1-Hydroxytricarballylate
  6. 1-Hydroxytricarballylic acid
  7. 3-Carboxy-2,3-dideoxy-1-hydroxypropan-1,2,3-tricarboxylate
  8. 3-Carboxy-2,3-dideoxy-1-hydroxypropan-1,2,3-tricarboxylic acid
  9. 3-carboxy-2,3-dideoxy-Pentarate
  10. 3-carboxy-2,3-dideoxy-Pentaric acid
  11. D-isocitrate
  12. I-CIT
  13. isocitrate
  14. threo-Ds-isocitrate
  15. threo-d(s)-iso-citrate
Chemical IUPAC Name 1-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 hydroxy acids
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • carboxylic acid
  • alpha-hydroxyacid
Biofunction
  • Component of Glutathione metabolism
Application
Source
  • Endogenous
Average Molecular Weight 192.124
Monoisotopic Molecular Weight 192.027008
Isomeric SMILES OC(C(CC(O)=O)C(O)=O)C(O)=O
Canonical SMILES OC(C(CC(O)=O)C(O)=O)C(O)=O
KEGG Compound ID C00311 Link Image
BioCyc ID threo-d(s)-iso-citrate Link Image
BiGG ID 34579 Link Image
Wikipedia Link Isocitric acid Link Image
NuGOwiki Link HMDB00193 Link Image
Metagene Link HMDB00193 Link Image
METLIN ID 3328 Link Image
PubChem Compound 1198 Link Image
PubChem Substance 668200 Link Image
ChEBI ID 16087 Link Image
CAS Registry Number 320-77-4
InChI Identifier InChI=1/C6H8O7/c7-3(8)1-2(5(10)11)4(9)6(12)13/h2,4,9H,1H2,(H,7,8)(H,10,11)(H,12,13)
Synthesis Reference Finogenova, T. V.; Kamzolova, S. V.; Dedyukhina, E. G.; Shishkanova, N. V.; Il'chenko, A. P.; Morgunov, I. G.; Chernyavskaya, O. G.; Sokolov, A. P. Biosynthesis of citric and isocitric acids from ethanol by mutant Yarrowia lipolytica N 1 under continuous cultivation. Applied Microbiology and Biotechnology (2002), 59(4-5), 493-500.
Melting Point (Experimental) 162-165 oC
Experimental Water Solubility 466 mg/mL [HMP experimental] Source: PhysProp
Predicted Water Solubility 52.5 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.35 [Predicted by ALOGPS]; -2.1 [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 1B0J 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 Not Available
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
  • mitochondria
  • peroxisome
Biofluid Location
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
  • Semen
  • Urine
Tissue Location
Tissue References
Adrenal Gland
Concentrations (Normal)
Biofluid Blood
Value 6.0 (0.0-10.0) 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 Cellular Cytoplasm
Value 38 (23-53) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
Biofluid CSF
Value 10.0 +/- 9.0 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 Semen
Value 400 - 1500 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Kavanagh JP: Isocitric and citric acid in human prostatic and seminal fluid: implications for prostatic metabolism and secretion. Prostate. 1994;24(3):139-42. [PubMed Link Image]
Biofluid Urine
Value 19.08 (5.26 - 42.76) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Sutor DJ, Percival JM: The estimation of D-isocitric acid in urine using isocitrate dehydrogenase. Clin Chim Acta. 1978 Jun;86(2):223-5. [PubMed Link Image]
Biofluid Urine
Value 94.3 (29.8-154.4) 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 120.1 (101.1-265.3) 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 53.7 (31.9-83.1) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments 2-6 years
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 45.0 (18.0-69.9) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments 6-10 years
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 38.9 (16.0-118.0) umol/mmol creatinine
Age Adult:>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 19.0 (5.0-34.0) 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. 130. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp. Basel, Switzerland c1981-1992.
Biofluid Urine
Value 7.7 (5.0-12.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
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 341 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Based on one measurement
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 Cellular Cytoplasm
Value 15 (14.8-15.2) uM
Age Adult:>18 yrs old
Sex Both
Condition Anoxia
Comments Not Available
References
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
Associated Disorders
Condition References
Anoxia
  • Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Citric Acid Cycle SMP00057 Link Image map00020 Link Image
General References
  1. Stromme JH, Borud O, Moe PJ: Fatal lactic acidosis in a newborn attributable to a congenital defect of pyruvate dehydrogenase. Pediatr Res. 1976 Jan;10(1):62-6. [PubMed Link Image]
  2. Zupke C, Sinskey AJ, Stephanopoulos G: Intracellular flux analysis applied to the effect of dissolved oxygen on hybridomas. Appl Microbiol Biotechnol. 1995 Dec;44(1-2):27-36. [PubMed Link Image]
  3. 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]
  4. Sutor DJ, Percival JM, Doonan S: Isolation and identification of some urinary inhibitors of calcium phosphate formation. Clin Chim Acta. 1978 Oct 16;89(2):273-8. [PubMed Link Image]
  5. Ebeling K, Ruckhaberle KE, Bilek K: [Studies on the recording of cytostatic effects on organ cultures of squamous cell carcinoma of the uterine cervix] Zentralbl Gynakol. 1977;99(20):1249-59. [PubMed Link Image]
  6. Sutor DJ, Percival JM, Doonan S: Urinary inhibitor of the formation of calcium oxalate. Br J Urol. 1979 Aug;51(4):253-5. [PubMed Link Image]
  7. Hennequin C, Lalanne V, Daudon M, Lacour B, Drueke T: A new approach to studying inhibitors of calcium oxalate crystal growth. Urol Res. 1993 Mar;21(2):101-8. [PubMed Link Image]
  8. Kavanagh JP: Isocitric and citric acid in human prostatic and seminal fluid: implications for prostatic metabolism and secretion. Prostate. 1994;24(3):139-42. [PubMed Link Image]
  9. Mikosha AS, Monissarenko VP, Bychkovskaia LA: [Properties of adrenocortical isocitrate dehydrogenase] Vopr Med Khim. 1981 Nov-Dec;27(6):736-9. [PubMed Link Image]
  10. 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]
  11. Sutor DJ, Percival JM: The estimation of D-isocitric acid in urine using isocitrate dehydrogenase. Clin Chim Acta. 1978 Jun;86(2):223-5. [PubMed Link Image]
  12. Wikipedia Link Image
Metabolic Enzymes
  1. Aconitate hydratase, mitochondrial precursor
  2. Iron-responsive element-binding protein 1
  3. Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial precursor
  4. Isocitrate dehydrogenase [NADP] cytoplasmic
  5. Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial precursor
  6. Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial precursor
  7. cDNA, FLJ96729, Homo sapiens isocitrate dehydrogenase 3 (NAD+) beta (IDH3B),nuclear gene encoding mitochondrial protein, transcript variant 1,mRNA (Isocitrate dehydrogenase 3 (NAD+) beta, isoform CRA_c)
  8. cDNA, FLJ93011, Homo sapiens isocitrate dehydrogenase 2 (NADP+), mitochondrial(IDH2), mRNA (Isocitrate dehydrogenase 2 (NADP+), mitochondrial, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 6000
Enzyme 1 Name Aconitate hydratase, mitochondrial precursor
Enzyme 1 Synonyms
  1. Citrate hydro-lyase
  2. Aconitase
Enzyme 1 Gene Name ACO2
Enzyme 1 Protein Sequence >Aconitate hydratase, mitochondrial precursor
MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLN
RPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAV
PSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILEN
YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSG
WSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYN
HRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHP
VAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGS
EQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRN
DANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPG
QDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAA
GPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVI
GDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHP
VDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ
Enzyme 1 Number of Residues 780
Enzyme 1 Molecular Weight 85426
Enzyme 1 Theoretical pI 7.65
Enzyme 1 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 1 General Function Energy production and conversion
Enzyme 1 Specific Function Citrate = cis-aconitate + H(2)O
Enzyme 1 Pathways
Enzyme 1 Reactions
  • citrate = cis-aconitate + H2O
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1718502 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q99798 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ACON_HUMAN Link Image
Enzyme 1 PDB ID 1B0J Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID U80040 Link Image
Enzyme 1 GeneCard ID ACO2 Link Image
Enzyme 1 GenAtlas ID ACO2 Link Image
Enzyme 1 HGNC ID HGNC:118 Link Image
Enzyme 1 Chromosome Location 22
Enzyme 1 Locus 22q11.2-q13.31|22q13.2-q13.31
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6001
Enzyme 2 Name Iron-responsive element-binding protein 1
Enzyme 2 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 2 Gene Name ACO1
Enzyme 2 Protein Sequence >Iron-responsive element-binding protein 1
MSNPFAHLAEPLDPVQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDI
ENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPA
DLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRIIPPGSGIIHQV
NLEYLARVVFDQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLP
QVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMC
PEYGATAAFFPVDEVSITYLVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQDPDFTQVVE
LDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKGFQVAPEHHNDHKTFIYDNT
EFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTY
YLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEG
RVHPNTRANYLASPPLVIAYAIAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVE
RQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPFFENLTLDLQPPK
SIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMA
RGTFANIRLLNRFLNKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSR
DWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTIIIP
ENLKPQMKVQVKLDTGKTFQAVMRFDTDVELTYFLNGGILNYMIRKMAK
Enzyme 2 Number of Residues 889
Enzyme 2 Molecular Weight 98400
Enzyme 2 Theoretical pI 6.66
Enzyme 2 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 2 General Function Energy production and conversion
Enzyme 2 Specific Function This protein also expresses aconitase activity
Enzyme 2 Pathways
Enzyme 2 Reactions
  • citrate = cis-aconitate + H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 33963 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P21399 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name IREB1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID Z11559 Link Image
Enzyme 2 GeneCard ID ACO1 Link Image
Enzyme 2 GenAtlas ID ACO1 Link Image
Enzyme 2 HGNC ID HGNC:117 Link Image
Enzyme 2 Chromosome Location 9
Enzyme 2 Locus 9p22-q32|9p22-p13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6179
Enzyme 3 Name Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial precursor
Enzyme 3 Synonyms
  1. Isocitric dehydrogenase
  2. NAD(+-specific ICDH
Enzyme 3 Gene Name IDH3B
Enzyme 3 Protein Sequence >Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial precursor
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVG
PELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPME
YKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESAR
GVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELY
PKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEY
AVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRT
RDMGGYSTTTDFIKSVIGHLQTKGS
Enzyme 3 Number of Residues 385
Enzyme 3 Molecular Weight 42184
Enzyme 3 Theoretical pI 8.66
Enzyme 3 GO Classification
Function
  • catalytic activity
  • isocitrate dehydrogenase (NAD+) activity
  • isocitrate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
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 3 General Function Energy production and conversion
Enzyme 3 Specific Function Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH
Enzyme 3 Pathways
Enzyme 3 Reactions
  • isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-25
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2737886 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O43837 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name IDH3B_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1158 bp
ATGGCGGTATTGAGCGGAGTCCGCTGGCTGACCCGAGCGCTGGTCTCCGCCGGGAACCCT
GGGGCATGGAGAGGTCTGAGTACCTCGGCCGCGGCGCACGCTGCATCGCGGAGCCAGGCC
GAGGACGTGAGGGTGGAGGGCTCCTTTCCCGTGACCATGCTTCCGGGAGACGGTGTGGGG
CCTGAGCTGATGCACGCCGTCAAGGAGGTGTTCAAGGCTGCCGCTGTCCCAGTGGAGTTC
CAGGAGCACCACCTGAGTGAGGTGCAGAATATGGCATCTGAGGAGAAGCTGGAGCAGGTG
CTGAGTTCCATGAAGGAGAACAAAGTGGCCATCATTGGAAAGATTCATACCCCGATGGAG
TATAAGGGGGAGCTAGCCTCCTATGATATGCGGCTGAGGCGTAAGTTGGACTTATTTGCC
AACGTAGTCCATGTGAAGTCACTTCCTGGGTATATGACTCGGCACAACAATCTAGACCTG
GTGATCATTCGAGAGCAGACAGAAGGGGAGTACAGCTCTCTGGAACATGAGAGTGCAAGG
GGTGTGATTGAGTGTTTGAAGATTGTCACACGAGCCAAGTCTCAGCGGATTGCAAAGTTC
GCCTTTGACTATGCCACCAAGAAGGGGCGGGGCAAGGTCACTGCTGTCCACAAGGCCAAC
ATCATGAAACTTGGGGATGGGTTGTTCCTGCAGTGCTGTGAGGAAGTTGCTGAACTGTAC
CCCAAAATCAAATTTGAGACAATGATCATAGACAACTGCTGCATGCAGCTGGTGCAGAAT
CCTTACCAGTTTGATGTGCTTGTGATGCCCAATCTCTATGGGAACATTATTGACAATCTG
GCTGCTGGCCTGGTTGGGGGAGCTGGTGTGGTCCCTGGTGAGAGCTATAGTGCAGAATAC
GCAGTCTTTGAGACGGGTGCCCGGCACCCATTTGCCCAGGCAGTGGGCAGGAATATAGCC
AATCCCACGGCCATGCTGCTGTCGGCTTCCAACATGCTGCGGCATCTTAATCTTGAGTAT
CACTCCAGCATGATCGCAGATGCGGTGAAGAAGGTGATCAAAGTTGGCAAGGTGCGGACT
CGAGACATGGGCGGCTACAGCACCACAACCGACTTCATCAAGTCTGTCATCGGTCACCTG
CAGACTAAAGGGAGCTAG
Enzyme 3 GenBank Gene ID U49283 Link Image
Enzyme 3 GeneCard ID IDH3B Link Image
Enzyme 3 GenAtlas ID IDH3B Link Image
Enzyme 3 HGNC ID HGNC:5385 Link Image
Enzyme 3 Chromosome Location 20
Enzyme 3 Locus 20p13
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6180
Enzyme 4 Name Isocitrate dehydrogenase [NADP] cytoplasmic
Enzyme 4 Synonyms
  1. Cytosolic NADP-isocitrate dehydrogenase
  2. Oxalosuccinate decarboxylase
  3. IDH
  4. NADP(+-specific ICDH
  5. IDP
Enzyme 4 Gene Name IDH1
Enzyme 4 Protein Sequence >Isocitrate dehydrogenase [NADP] cytoplasmic
MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDA
AEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRL
VSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAM
GMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFE
AQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDG
KTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALE
EVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL
Enzyme 4 Number of Residues 414
Enzyme 4 Molecular Weight 46660
Enzyme 4 Theoretical pI 7.00
Enzyme 4 GO Classification
Function
  • catalytic activity
  • isocitrate dehydrogenase (NADP+) activity
  • isocitrate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • main pathways of carbohydrate metabolism
  • metabolism
  • physiological process
Component
Enzyme 4 General Function Energy production and conversion
Enzyme 4 Specific Function Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH
Enzyme 4 Pathways
Enzyme 4 Reactions
  • isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 3641398 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O75874 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name IDHC_HUMAN Link Image
Enzyme 4 PDB ID 1T0L Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1245 bp
ATGTCCAAAAAAATCAGTGGCGGTTCTGTGGTAGAGATGCAAGGAGATGAAATGACACGA
ATCATTTGGGAATTGATTAAAGAGAAACTCATTTTTCCCTACGTGGAATTGGATCTACAT
AGCTATGATTTAGGCATAGAGAATCGTGATGCCACCAACGACCAAGTCACCAAGGATGCT
GCAGAAGCTATAAAGAAGCATAATGTTGGCGTCAAATGTGCCACTATCACTCCTGATGAG
AAGAGGGTTGAGGAGTTCAAGTTGAAACAAATGTGGAAATCACCAAATGGCACCATACGA
AATATTCTGGGTGGCACGGTCTTCAGAGAAGCCATTATCTGCAAAAATATCCCCCGGCTT
GTGAGTGGATGGGTAAAACCTATCATCATAGGTCGTCATGCTTATGGGGATCAATACAGA
GCAACTGATTTTGTTGTTCCTGGGCCTGGAAAAGTAGAGATAACCTACACACCAAGTGAC
GGAACCCAAAAGGTGACATACCTGGTACATAACTTTGAAGAAGGTGGTGGTGTTGCCATG
GGGATGTATAATCAAGATAAGTCAATTGAAGATTTTGCACACAGTTCCTTCCAGATGGCT
CTGTCTAAGGGTTGGCCTTTGTATCTGAGCACCAAAAACACTATTCTGAAGATATATGAT
GGGCGTTTTAAAGACATCTTTCAGGAGATATATGACAAGCAGTACAAGTCCCAGTTTGAA
GCTCAAAAGATCTGGTATGAGCATAGGCTCATCGACGACATGGTGGCCCAAGCTATGAAA
TCAGAGGGAGGCTTCATCTGGGCCTGTAAAAACTATGATGGTGACGTGCAGTCGGACTCT
GTGGCCCAAGGGTATGGCTCTCTCGGCATGATGACCAGCGTGCTGGTTTGTCCAGATGGC
AAGACAGTAGAAGCAGAGGCTGCCCACGGGACTGTAACCCGTCACTACCGCATGTACCAG
AAAGGACAGGAGACGTCCACCAACCTCATTGCTTCCATTTTTGCCTGGACCAGAGGGTTA
GCCCACAGAGCAAAGCTTGATAACAATAAAGAGCTTGCCTTCTTTGCAAATGCTTTGGAA
GAAGTCTCTATTGAGACAATTGAGGCTGGCTTCATGACCAAGGACTTGGCTGCTTGCATT
AGAGGTTTACCCAATGTGCAACGTTCTGACTACTTGAATACATTTGAGTTCATGGATAAA
CTTGGAGAAAACTTGAAGATCAAACTAGCTCAGGCCAAACTTTAA
Enzyme 4 GenBank Gene ID AF020038 Link Image
Enzyme 4 GeneCard ID IDH1 Link Image
Enzyme 4 GenAtlas ID IDH1 Link Image
Enzyme 4 HGNC ID HGNC:5382 Link Image
Enzyme 4 Chromosome Location 2
Enzyme 4 Locus 2q33.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Nekrutenko A, Hillis DM, Patton JC, Bradley RD, Baker RJ: Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family. Mol Biol Evol. 1998 Dec;15(12):1674-84. [PubMed Link Image]
  2. Geisbrecht BV, Gould SJ: The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase. J Biol Chem. 1999 Oct 22;274(43):30527-33. [PubMed Link Image]
  3. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 6181
Enzyme 5 Name Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial precursor
Enzyme 5 Synonyms
  1. Isocitric dehydrogenase
  2. NAD(+-specific ICDH
Enzyme 5 Gene Name IDH3A
Enzyme 5 Protein Sequence >Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial precursor
MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAP
IQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDL
YANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIA
EFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAESCKDIKFNEMYLDTVCLNMV
QDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKD
MANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICR
RVKDLD
Enzyme 5 Number of Residues 366
Enzyme 5 Molecular Weight 39592
Enzyme 5 Theoretical pI 6.93
Enzyme 5 GO Classification
Function
  • catalytic activity
  • isocitrate dehydrogenase (NAD+) activity
  • isocitrate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
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 5 General Function Energy production and conversion
Enzyme 5 Specific Function Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH
Enzyme 5 Pathways
Enzyme 5 Reactions
  • isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 706839 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P50213 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name IDH3A_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1101 bp
ATGGCTGGGCCCGCGTGGATCTCCAAGGTCTCTCGGCTGCTGGGGGCATTCCACAACCCA
AAACAGGTGACCAGAGGTTTTACTGGTGGTGTTCAGACAGTAACTTTAATTCCAGGAGAT
GGTATTGGCCCAGAAATTTCAGCTGCAGTTATGAAGATTTTTGATGCTGCCAAAGCACCT
ATTCAGTGGGAGGAGCGGAACGTCACTGCCATTCAAGGACCTGGAGGAAAGTGGATGATC
CCTTCAGAGGCTAAAGAGTCCATGGATAAGAACAAGATGGGCTTGAAAGGCCCTTTGAAG
ACCCCAATAGCAGCCGGTCACCCATCTATGAATTTACTGCTGCGCAAAACATTTGACCTT
TACGCGAATGTCCGACCATGTGTCTCTATCGAAGGCTATAAAACCCCTTACACCGATGTA
AATATTGTGACCATTCGAGAGAACACAGAAGGAGAATACAGTGGAATTGAGCATGTGATT
GTTGATGGAGTCGTGCAGAGTATCAAGCTCATCACCGAGGGGGCGAGCAAGCGCATTGCT
GAGTTTGCCTTTGAGTATGCCCGGAACAACCACCGGAGCAACGTCACGGCGGTGCACAAA
GCCAACATCATGCGGATGTCAGATGGGCTTTTTCTACAAAAATGCAGGGAAGTTGCAGAA
AGCTGTAAAGATATTAAATTTAATGAGATGTACCTTGATACAGTATGTTTGAATATGGTA
CAAGATCCTTCCCAATTTGATGTTCTTGTTATGCCAAATTTGTATGGAGACATCCTTAGT
GACTTGTGTGCAGGATTGATCGGAGGTCTCGGTGTGACACCAAGTGGCAACATTGGAGCC
AATGGGGTTGCAATTTTTGAGTCGGTTCATGGGACGGCTCCAGACATTGCAGGCAAGGAC
ATGGCGAATCCCACAGCCCTCCTGCTCAGTGCCGTGATGATGCTGCGCCACATGGGACTT
TTTGACCATGCTGCAAGAATTGAGGCTGCGTGTTTTGCTACAATTAAGGACGGAAAGAGC
TTGACAAAAGATTTGGGAGGCAATGCAAAATGCTCAGACTTCACAGAGGAAATCTGTCGC
CGAGTAAAAGATTTAGATTAA
Enzyme 5 GenBank Gene ID U07681 Link Image
Enzyme 5 GeneCard ID IDH3A Link Image
Enzyme 5 GenAtlas ID IDH3A Link Image
Enzyme 5 HGNC ID HGNC:5384 Link Image
Enzyme 5 Chromosome Location 15
Enzyme 5 Locus 15q25.1-q25.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Kim YO, Oh IU, Park HS, Jeng J, Song BJ, Huh TL: Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species. Biochem J. 1995 May 15;308 ( Pt 1):63-8. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 6182
Enzyme 6 Name Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial precursor
Enzyme 6 Synonyms
  1. Isocitric dehydrogenase
  2. NAD(+-specific ICDH
Enzyme 6 Gene Name IDH3G
Enzyme 6 Protein Sequence >Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial precursor
MALKVATVAGSAAKAVLGPALLCRPWEVLGAHEVPSRNIFSEQTIPPSAKYGGRHTVTMI
PGDGIGPELMLHVKSVFRHACVPVDFEEVHVSSNADEEDIRNAIMAIRRNRVALKGNIET
NHNLPPSHKSRNNILRTSLDLYANVIHCKSLPGVVTRHKDIDILIVRENTEGEYSSLEHE
SVAGVVESLKIITKAKSLRIAEYAFKLAQESGRKKVTAVHKANIMKLGDGLFLQCCREVA
ARYPQITFENMIVDNTTMQLVSRPQQFDVMVMPNLYGNIVNNVCAGLVGGPGLVAGANYG
HVYAVFETATRNTGKSIANKNIANPTATLLASCMMLDHLKLHSYATSIRKAVLASMDNEN
MHTPDIGGQGTTSEAIQDVIRHIRVINGRAVEA
Enzyme 6 Number of Residues 393
Enzyme 6 Molecular Weight 42795
Enzyme 6 Theoretical pI 8.66
Enzyme 6 GO Classification
Function
  • catalytic activity
  • isocitrate dehydrogenase (NAD+) activity
  • isocitrate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
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 6 General Function Energy production and conversion
Enzyme 6 Specific Function Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH
Enzyme 6 Pathways
Enzyme 6 Reactions
  • isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-30
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 1167849 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P51553 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name IDH3G_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1182 bp
ATGGCGCTGAAGGTAGCGACCGTCGCCGGCAGCGCCGCGAAGGCGGTGCTCGGGCCAGCC
CTTCTCTGCCGTCCCTGGGAGGTTCTAGGCGCCCACGAGGTCCCCTCGAGGAACATCTTT
TCAGAACAAACAATTCCTCCGTCCGCTAAGTATGGCGGGCGGCACACGGTGACCATGATC
CCAGGGGATGGCATCGGGCCAGAGCTCATGCTGCATGTCAAGTCCGTCTTCAGGCACGCA
TGTGTACCAGTGGACTTTGAAGAGGTGCACGTGAGTTCCAATGCTGATGAAGAGGACATT
CGCAATGCCATCATGGCCATCCGCCGGAACCGCGTGGCCCTGAAGGGCAACATCGAAACC
AACCATAACCTGCCACCGTCGCACAAATCTCGAAACAACATCCTTCGCACCAGCCTGGAC
CTCTATGCCAACGTCATCCACTGTAAGAGCCTTCCAGGCGTGGTGACCCGGCACAAGGAC
ATAGACATCCTCATTGTCCGGGAGAACACAGAGGGCGAGTACAGCAGCCTGGAGCATGAG
AGTGTGGCGGGAGTGGTGGAGAGCCTGAAGATCATCACCAAGGCCAAGTCCCTGCGCATT
GCCGAGTATGCCTTCAAGCTGGCGCAGGAGAGCGGGCGCAAGAAAGTGACGGCCGTGCAC
AAGGCCAACATCATGAAACTGGGCGATGGGCTTTTCCTCCAGTGCTGCAGGGAGGTGGCA
GCCCGCTACCCTCAGATCACCTTCGAGAACATGATTGTGGATAACACCACCATGCAGCTG
GTGTCCCGGCCCCAGCAGTTTGATGTCATGGTGATGCCCAATCTCTATGGCAACATCGTC
AACAATGTCTGCGCGGGACTGGTCGGGGGCCCAGGCCTTGTGGCTGGGGCCAACTATGGC
CATGTGTACGCGGTGTTTGAAACAGCTACGAGGAACACCGGCAAGAGTATCGCCAATAAG
AACATCGCCAACCCCACGGCCACCCTGCTGGCCAGCTGCATGATGCTGGACCACCTCAAG
CTGCACTCCTATGCCACCTCCATCCGTAAGGCTGTCCTGGCATCCATGGACAATGAGAAT
ATGCACACTCCGGACATCGGGGGCCAGGGCACAACATCTGAAGCCATCCAGGACGTCATC
CGCCACATCCGCGTCATCAACGGCCGGGCCGTGGAGGCCTAG
Enzyme 6 GenBank Gene ID Z68907 Link Image
Enzyme 6 GeneCard ID IDH3G Link Image
Enzyme 6 GenAtlas ID IDH3G Link Image
Enzyme 6 HGNC ID HGNC:5386 Link Image
Enzyme 6 Chromosome Location X
Enzyme 6 Locus Xq28
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Brenner V, Nyakatura G, Rosenthal A, Platzer M: Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse. Genomics. 1997 Aug 15;44(1):8-14. [PubMed Link Image]
  2. Kim YO, Koh HJ, Kim SH, Jo SH, Huh JW, Jeong KS, Lee IJ, Song BJ, Huh TL: Identification and functional characterization of a novel, tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta subunit isoform. J Biol Chem. 1999 Dec 24;274(52):36866-75. [PubMed Link Image]
  3. Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S: Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep. 2000 Sep;1(3):287-92. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16508
Enzyme 7 Name cDNA, FLJ96729, Homo sapiens isocitrate dehydrogenase 3 (NAD+) beta (IDH3B),nuclear gene encoding mitochondrial protein, transcript variant 1,mRNA (Isocitrate dehydrogenase 3 (NAD+) beta, isoform CRA_c)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name IDH3B
Enzyme 7 Protein Sequence >cDNA, FLJ96729, Homo sapiens isocitrate dehydrogenase 3 (NAD+) beta (IDH3B),nuclear gene encoding mitochondrial protein, transcript variant 1,mRNA (Isocitrate dehydrogenase 3 (NAD+) beta, isoform CRA_c)
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVG
PELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPME
YKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESAR
GVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELY
PKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEY
AVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRT
RDMGGYSTTTDFIKSVIGHLQTKGS
Enzyme 7 Number of Residues 385
Enzyme 7 Molecular Weight 42184
Enzyme 7 Theoretical pI 8.66
Enzyme 7 GO Classification
Function
  • catalytic activity
  • isocitrate dehydrogenase (NAD+) activity
  • isocitrate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
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 7 General Function Energy production and conversion
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID B2RDR1 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name B2RDR1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence Not Available
Enzyme 7 GenBank Gene ID AK315641 Link Image
Enzyme 7 GeneCard ID B2RDR1 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location 20
Enzyme 7 Locus 20p13
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16509
Enzyme 8 Name cDNA, FLJ93011, Homo sapiens isocitrate dehydrogenase 2 (NADP+), mitochondrial(IDH2), mRNA (Isocitrate dehydrogenase 2 (NADP+), mitochondrial, isoform CRA_a)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name IDH2
Enzyme 8 Protein Sequence >cDNA, FLJ93011, Homo sapiens isocitrate dehydrogenase 2 (NADP+), mitochondrial(IDH2), mRNA (Isocitrate dehydrogenase 2 (NADP+), mitochondrial, isoform CRA_a)
MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPVVEMDGDEMTR
IIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDE
ARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYK
ATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAI
QKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKS
SGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQK
GRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEKVCVETVESGAMTKDLAGCIH
GLSNVKLNEHFLNTTDFLDTIKSNLDRALGRQ
Enzyme 8 Number of Residues 452
Enzyme 8 Molecular Weight 50910
Enzyme 8 Theoretical pI 8.95
Enzyme 8 GO Classification
Function
  • catalytic activity
  • isocitrate dehydrogenase (NADP+) activity
  • isocitrate dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • main pathways of carbohydrate metabolism
  • metabolism
  • physiological process
Component
Enzyme 8 General Function Energy production and conversion
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID B2R6L6 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name B2R6L6_HUMAN Link Image
Enzyme 8 PDB ID 1LWD Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence Not Available
Enzyme 8 GenBank Gene ID AK312627 Link Image
Enzyme 8 GeneCard ID B2R6L6 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location 15
Enzyme 8 Locus 15q26.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available