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Human Metabolome Database Version 2.5

 

Showing metabocard for cis-Aconitic acid (HMDB00072)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-28 13:51:25
Accession Number HMDB00072
Secondary Accession Numbers HMDB00461
Common Name cis-Aconitic acid
Description An intermediate in the tricarboxylic acid cycle produced by the dehydration of citric acid. The enzyme aconitase (aconitate hydratase; EC 4.2.1.3) catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle
Synonyms
  1. (1Z)-1-Propene-1,2,3-tricarboxylate
  2. (1Z)-1-Propene-1,2,3-tricarboxylic acid
  3. (Z)-1-Propene-1,2,3-tricarboxylate
  4. (Z)-1-Propene-1,2,3-tricarboxylic acid
  5. (Z)-Aconitate
  6. (Z)-Aconitic acid
  7. 1-cis-2,3-Propenetricarboxylate
  8. 1-cis-2,3-Propenetricarboxylic acid
  9. 1-propene-1,2,3-tricarboxylate
  10. 1-propene-1,2,3-tricarboxylic acid
  11. cis-1-Propene-1,2,3-tricarboxylate
  12. cis-1-Propene-1,2,3-tricarboxylic acid
  13. cis-Aconate
  14. cis-Aconic acid
  15. cis-Aconitate
  16. cis-Aconitic acid
  17. cis-Oxaloacetate
  18. cis-Oxaloacetic acid
Chemical IUPAC Name (1Z)-1-Propene-1,2,3-tricarboxylic acid
Chemical Formula C6H6O6
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Organic acids
Class
  • Tricarboxylic Acids
Sub Class
  • Short chain tricarboxylic acids
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • alkene
Biofunction
  • Component of Glyoxylate and dicarboxylate metabolism
Application
Source
  • Endogenous
Average Molecular Weight 174.108
Monoisotopic Molecular Weight 174.016434
Isomeric SMILES OC(=O)CC(=CC(O)=O)C(O)=O
Canonical SMILES OC(=O)CC(=CC(O)=O)C(O)=O
KEGG Compound ID C00417 Link Image
BioCyc ID CIS-ACONITATE Link Image
BiGG ID Not Available
Wikipedia Link Not Available
NuGOwiki Link HMDB00072 Link Image
Metagene Link HMDB00072 Link Image
METLIN ID 5130 Link Image
PubChem Compound 309 Link Image
PubChem Substance 3707 Link Image
ChEBI ID 32805 Link Image
CAS Registry Number 585-84-2
InChI Identifier InChI=1/C6H6O6/c7-4(8)1-3(6(11)12)2-5(9)10/h1H,2H2,(H,7,8)(H,9,10)(H,11,12)/b3-1-
Synthesis Reference Gutierrez, Eddie N.; Lamberti, Vincent. cis and trans Aconitic acids and their salts. U.S. (1978), 16 pp.
Melting Point (Experimental) 125 oC
Experimental Water Solubility 400.0 mg/mL [BEILSTEIN] Source: PhysProp
Predicted Water Solubility 6.72 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.41 [Predicted by ALOGPS]; -1.1 [Predicted by PubChem via XLOGP]; -0.14 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
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
Biofluid Location
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid CSF
Value 20.0 (13.0-27.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Redjems-Bennani N, Jeandel C, Lefebvre E, Blain H, Vidailhet M, Gueant JL: Abnormal substrate levels that depend upon mitochondrial function in cerebrospinal fluid from Alzheimer patients. Gerontology. 1998;44(5):300-4. [PubMed Link Image]
Biofluid CSF
Value 2 uM
Age Children:1-13 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 Urine
Value 54.5 (32.4-76.6) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
Biofluid Urine
Value 67.9 (14.3-100.7) 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 73.8 (64.0-130.3) 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 37.9 (17.3-63.3) 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 29.8 (14.7-93.1) 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 35.95 umol/mmol creatinine
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 Urine
Value 32.0 (0.0-70.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Lung Cancer
Comments Not Available
References
  • HMP experimental
Associated Disorders
Condition References
Lung Cancer
  • HMP experimental
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Citric Acid Cycle SMP00057 Link Image map00020 Link Image
General References
  1. Swart PJ, Kuipers EM, Smit C, Van Der Strate BW, Harmsen MC, Meijer DK: Lactoferrin. Antiviral activity of lactoferrin. Adv Exp Med Biol. 1998;443:205-13. [PubMed Link Image]
  2. 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]
  3. Boulat O, Gradwohl M, Matos V, Guignard JP, Bachmann C: Organic acids in the second morning urine in a healthy Swiss paediatric population. Clin Chem Lab Med. 2003 Dec;41(12):1642-58. [PubMed Link Image]
  4. 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]
  5. Redjems-Bennani N, Jeandel C, Lefebvre E, Blain H, Vidailhet M, Gueant JL: Abnormal substrate levels that depend upon mitochondrial function in cerebrospinal fluid from Alzheimer patients. Gerontology. 1998;44(5):300-4. [PubMed Link Image]
  6. Swart PJ, Kuipers ME, Smit C, Pauwels R, deBethune MP, de Clercq E, Meijer DK, Huisman JG: Antiviral effects of milk proteins: acylation results in polyanionic compounds with potent activity against human immunodeficiency virus types 1 and 2 in vitro. AIDS Res Hum Retroviruses. 1996 Jun 10;12(9):769-75. [PubMed Link Image]
  7. Matsuishi T, Urabe F, Percy AK, Komori H, Yamashita Y, Schultz RS, Ohtani Y, Kuriya N, Kato H: Abnormal carbohydrate metabolism in cerebrospinal fluid in Rett syndrome. J Child Neurol. 1994 Jan;9(1):26-30. [PubMed Link Image]
Metabolic Enzymes
  1. Aconitate hydratase, mitochondrial
  2. Cytoplasmic aconitate hydratase
Enzyme 1 [top]
Enzyme 1 ID 6000
Enzyme 1 Name Aconitate hydratase, mitochondrial
Enzyme 1 Synonyms
  1. Aconitase
  2. Citrate hydro-lyase
Enzyme 1 Gene Name ACO2
Enzyme 1 Protein Sequence >Aconitate hydratase, mitochondrial
MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLN
RPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAV
PSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILEN
YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSG
WSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYN
HRMKKYLSKTGREDIANLADEFKDHLVPDPGCHYDQLIEINLSELKPHINGPFTPDLAHP
VAEVGKVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGS
EQIRATIERDGYAQILRDLGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRN
DANPETHAFVTSPEIVTALAIAGTLKFNPETDYLTGTDGKKFRLEAPDADELPKGEFDPG
QDTYQHPPKDSSGQHVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAA
GPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVI
GDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPADYNKIHP
VDKLTIQGLKDFTPGKPLKCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ
Enzyme 1 Number of Residues 780
Enzyme 1 Molecular Weight 85424.7
Enzyme 1 Theoretical pI 7.65
Enzyme 1 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • aconitate hydratase activity
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • iron-sulfur cluster binding
  • lyase activity
  • metal cluster binding
Process
  • acetyl-CoA catabolic process
  • acetyl-CoA metabolic process
  • cellular metabolic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • metabolic process
  • tricarboxylic acid cycle
Component
Enzyme 1 General Function Involved in metabolic process
Enzyme 1 Specific Function Citrate = isocitrate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (1) citrate = isocitrate [RN:R01324]
  • (2) (1a) citrate = cis-aconitate + H2O [RN:R01325]
  • (3) (1b) cis-aconitate + H2O = isocitrate [RN:R01900]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 55957148 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
CATGTGGCCTCAGTCCTGTGCCAACGGGCCAAGGTGGCGATGAGCCACTTTGAGCCCAAC
GAGTACATCCATTATGACCTGCTAGAGAAGAACATTAACATTGTTCGCAAACGACTGAAC
CGGCCGCTGACACTCTCGGAGAAGATTGTGTATGGACACCTGGATGACCCCGCCAGCCAG
GAAATTGAGCGAGGCAAGTCGTACCTGCGGCTGCGGCCGGACCGTGTGGCCATGCAGGAT
GCGACGGCCCAGATGGCCATGCTCCAGTTCATCAGCAGCGGGCTGTCCAAGGTGGCTGTG
CCATCCACCATCCACTGTGACCATCTGATTGAAGCCCAGGTTGGGGGCGAGAAAGACCTG
CGCCGGGCCAAGGACATCAACCAGGAAGTTTATAATTTCCTGGCAACTGCAGGTGCCAAA
TATGGCGTGGGCTTCTGGAAGCCTGGATCTGGAATCATTCACCAGATTATTCTGGAAAAC
TATGCGTACCCTGGTGTTCTTCTGATTGGCACTGACTCCCACACCCCCAATGGTGGCGGC
CTTGGGGGCATCTGCATTGGAGTTGGGGGTGCCGATGCTGTGGATGTCATGGCTGGGATC
CCCTGGGAGCTGAAGTGCCCCAAGGTGATTGGCGTGAAGCTGACGGGCTCTCTCTCCGGT
TGGTCCTCACCCAAAGATGTGATCCTGAAGGTGGCAGGCATCCTCACGGTGAAAGGTGGC
ACAGGTGCAATCGTGGAATACCACGGGCCTGGTGTAGACTCCATCTCCTGCACTGGCATG
GCGACAATCTGCAACATGGGTGCAGAAATTGGGGCCACCACTTCCGTGTTCCCTTACAAC
CACAGGATGAAGAAGTACCTGAGCAAGACCGGCCGGGAAGACATTGCCAATCTAGCTGAT
GAATTCAAGGATCACTTGGTGCCTGACCCTGGCTGCCATTATGACCAACTAATTGAAATT
AACCTCAGTGAGCTGAAGCCACACATCAATGGGCCCTTCACCCCTGACCTGGCTCACCCT
GTGGCAGAAGTGGGCAAGGTGGCAGAGAAGGAAGGATGGCCTCTGGACATCCGAGTGGGT
CTAATTGGTAGCTGCACCAATTCAAGCTATGAAGATATGGGGCGCTCAGCAGCTGTGGCC
AAGCAGGCACTGGCCCATGGCCTCAAGTGCAAGTCCCAGTTCACCATCACTCCAGGTTCC
GAGCAGATCCGCGCCACCATTGAGCGGGACGGCTATGCACAGATCTTGAGGGATCTGGGT
GGCATTGTCCTGGCCAATGCTTGTGGCCCCTGCATTGGCCAGTGGGACAGGAAGGACATC
AAGAAGGGGGAGAAGAACACAATCGTCACCTCCTACAACAGGAACTTCACGGGCCGCAAC
GACGCAAACCCCGAGACCCATGCCTTTGTCACGTCCCCAGAGATTGTCACAGCCCTGGCC
ATTGCGGGAACCCTCAAGTTCAACCCAGAGACCGACTACCTGACGGGCACGGATGGCAAG
AAGTTCAGGCTGGAGGCTCCGGATGCAGATGAGCTTCCCAAAGGGGAGTTTGACCCAGGG
CAGGACACCTACCAGCACCCACCCAAGGACAGCAGCGGGCAGCATGTGGACGTGAGCCCC
ACCAGCCAGCGCCTGCAGCTCCTGGAGCCTTTTGACAAGTGGGATGGCAAGGACCTGGAG
GACCTGCAGATCCTCATCAAGGTCAAAGGGAAGTGTACCACTGACCACATCTCAGCTGCT
GGCCCCTGGCTCAAGTTCCGTGGGCACTTGGATAACATCTCCAACAACCTGCTCATTGGT
GCCATCAACATTGAAAACGGCAAGGCCAACTCCGTGCGCAATGCCGTCACTCAGGAGTTT
GGCCCCGTCCCTGACACTGCCCGCTACTACAAGAAACATGGCATCAGGTGGGTGGTGATC
GGAGACGAGAACTACGGCGAGGGCTCGAGCCGGGAGCATGCAGCTCTGGAGCCTCGCCAC
CTTGGGGGCCGGGCCATCATCACCAAGAGCTTTGCCAGGATCCACGAGACCAACCTGAAG
AAACAGGGCCTGCTGCCTCTGACCTTCGCTGACCCGGCTGACTACAACAAGATTCACCCT
GTGGACAAGCTGACCATTCAGGGCCTGAAGGACTTCACCCCTGGCAAGCCCCTGAAGTGC
ATCATCAAGCACCCCAACGGGACCCAGGAGACCATCCTCCTGAACCACACCTTCAACGAG
ACGCAGATTGAGTGGTTCCGCGCTGGCAGTGCCCTCAACAGAATGAAGGAACTGCAACAG
TGA
Enzyme 1 GenBank Gene ID AL008582 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 2
Enzyme 1 Locus 22q11.2-q13.31|22q13.2
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. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Baldwin GS, Seet KL, Callaghan J, Toncich G, Toh BH, Moritz RL, Rubira MR, Simpson R: Purification and partial amino acid sequence of human aconitase. Protein Seq Data Anal. 1991 Aug;4(2):63-7. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6001
Enzyme 2 Name Cytoplasmic aconitate hydratase
Enzyme 2 Synonyms
  1. Aconitase
  2. Citrate hydro-lyase
  3. Ferritin repressor protein
  4. Iron regulatory protein 1
  5. IRP1
  6. Iron-responsive element-binding protein 1
  7. IRE-BP 1
Enzyme 2 Gene Name ACO1
Enzyme 2 Protein Sequence >Cytoplasmic aconitate hydratase
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 98398.1
Enzyme 2 Theoretical pI 6.66
Enzyme 2 GO Classification
Function
  • 4 iron, 4 sulfur cluster binding
  • binding
  • iron-sulfur cluster binding
  • metal cluster binding
Process
  • metabolic process
Component
Enzyme 2 General Function Involved in metabolic process
Enzyme 2 Specific Function Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (1) citrate = isocitrate [RN:R01324]
  • (2) (1a) citrate = cis-aconitate + H2O [RN:R01325]
  • (3) (1b) cis-aconitate + H2O = isocitrate [RN:R01900]
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 ACOC_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|9p21.1
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. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. 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]
  6. 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]
  7. Philpott CC, Klausner RD, Rouault TA: The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7321-5. [PubMed Link Image]
  8. Vashisht AA, Zumbrennen KB, Huang X, Powers DN, Durazo A, Sun D, Bhaskaran N, Persson A, Uhlen M, Sangfelt O, Spruck C, Leibold EA, Wohlschlegel JA: Control of iron homeostasis by an iron-regulated ubiquitin ligase. Science. 2009 Oct 30;326(5953):718-21. Epub 2009 Sep 17. [PubMed Link Image]
  9. Salahudeen AA, Thompson JW, Ruiz JC, Ma HW, Kinch LN, Li Q, Grishin NV, Bruick RK: An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis. Science. 2009 Oct 30;326(5953):722-6. Epub 2009 Sep 17. [PubMed Link Image]
  10. Condo I, Malisan F, Guccini I, Serio D, Rufini A, Testi R: Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin. Hum Mol Genet. 2010 Apr 1;19(7):1221-9. Epub 2010 Jan 6. [PubMed Link Image]
  11. Dupuy J, Volbeda A, Carpentier P, Darnault C, Moulis JM, Fontecilla-Camps JC: Crystal structure of human iron regulatory protein 1 as cytosolic aconitase. Structure. 2006 Jan;14(1):129-39. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available