|
Enzyme 1
[top]
|
| Enzyme 1 ID |
6000 |
| Enzyme 1 Name |
Aconitate hydratase, mitochondrial |
| Enzyme 1 Synonyms |
- Aconitase
- 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 |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
55957148  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q99798  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ACON_HUMAN  |
| Enzyme 1 PDB ID |
1B0J  |
| 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  |
| Enzyme 1 GeneCard ID |
ACO2  |
| Enzyme 1 GenAtlas ID |
ACO2  |
| Enzyme 1 HGNC ID |
HGNC:118  |
| Enzyme 1 Chromosome Location |
2 |
| Enzyme 1 Locus |
22q11.2-q13.31|22q13.2 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
6001 |
| Enzyme 2 Name |
Cytoplasmic aconitate hydratase |
| Enzyme 2 Synonyms |
- Aconitase
- Citrate hydro-lyase
- Ferritin repressor protein
- Iron regulatory protein 1
- IRP1
- Iron-responsive element-binding protein 1
- 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 |
|
| 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 |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
33963  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P21399  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ACOC_HUMAN  |
| 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  |
| Enzyme 2 GeneCard ID |
ACO1  |
| Enzyme 2 GenAtlas ID |
ACO1  |
| Enzyme 2 HGNC ID |
HGNC:117  |
| Enzyme 2 Chromosome Location |
9 |
| Enzyme 2 Locus |
9p22-q32|9p21.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6178 |
| Enzyme 3 Name |
Isocitrate dehydrogenase [NADP], mitochondrial |
| Enzyme 3 Synonyms |
- IDH
- ICD-M
- IDP
- NADP(+)-specific ICDH
- Oxalosuccinate decarboxylase
|
| Enzyme 3 Gene Name |
IDH2 |
| Enzyme 3 Protein Sequence |
>Isocitrate dehydrogenase [NADP], mitochondrial
MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPVVEMDGDEMTR
IIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDSALATQKYSVAVKCATITPDE
ARVEEFKLKKMWKSPNGTIRNILGGTVFREPIICKNIPRLVPGWTKPITIGRHAHGDQYK
ATDFVADRAGTFKMVFTPKDGSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAI
QKKWPLYMSTKNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKS
SGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGTVTRHYREHQK
GRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEKVCVETVESGAMTKDLAGCIH
GLSNVKLNEHFLNTTDFLDTIKSNLDRALGRQ
|
| Enzyme 3 Number of Residues |
452 |
| Enzyme 3 Molecular Weight |
50908.9 |
| Enzyme 3 Theoretical pI |
8.95 |
| Enzyme 3 GO Classification |
| Function |
- NAD or NADH binding
- binding
- catalytic activity
- cation binding
- ion binding
- isocitrate dehydrogenase (NADP+) activity
- isocitrate dehydrogenase activity
- magnesium ion binding
- metal ion binding
- nucleotide binding
- 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 |
- carboxylic acid metabolic process
- cellular metabolic process
- isocitrate metabolic process
- metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in magnesium ion binding |
| Enzyme 3 Specific Function |
Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- (1) isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+ (overall reaction) [RN:R00267]
- (2) (1a) isocitrate + NADP+ = oxalosuccinate + NADPH + H+ [RN:R01899]
- (3) (1b) oxalosuccinate = 2-oxoglutarate + CO2 [RN:R00268]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
872121  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P48735  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
IDHP_HUMAN  |
| Enzyme 3 PDB ID |
1LWD  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1359 bp
ATGGCCGGCTACCTGCGGGTCGTGCGCTCGCTCTGCAGAGCCTCAGGCTCGCGGCCGGCC
TGGGCGCCGGCGGCCCTGACAGCCCCCACCTCGCAAGAGCATCCGCGGCGCCACTATGCC
GACAAAAGGATCAAGGTGGCGAAGCCCGTGGTGGAGATGGATGGTGATGAGATGACCCGT
ATTATCTGGCAGTTCATCAAGGAGAAGCTCATCCTGCCCCACGTGGACATCCAGCTAAAG
TATTTTGACCTCGGGCTCCCAAACCGTGACCAGACTGATGACCAGGTCACCATTGACTCT
GCACTGGCCACCCAGAAGTACAGTGTGGCTGTCAAGTGTGCCACCATCACCCCTGATGAG
GCCCGTGTGGAAGAGTTCAAGCTGAAGAAGATGTGGAAAAGTCCCAATGGAACTATCCGG
AACATCCTGGGGGGGACTGTCTTCCGGGAGCCCATCATCTGCAAAAACATCCCACGCCTA
GTCCCTGGCTGGACCAAGCCCATCACCATTGGCAGGCACGCCCATGGCGACCAGTACAAG
GCCACAGACTTTGTGGCAGACCGGGCCGGCACTTTCAAAATGGTCTTCACCCCAAAAGAT
GGCAGTGGTGTCAAGGAGTGGGAAGTGTACAACTTTCCCGCAGGCGGCGTGGGCATGGGC
ATGTACAACACCGACGAGTCCATCTCAGGTTTTGCGCACAGCTGCTTCCAGTATGCCATC
CAGAAGAAATGGCCGCTGTACATGAGCACCAAGAACACCATACTGAAAGCCTACGATGGG
CGTTTCAAGGACATCTTCCAGGAGATCTTTGACAAGCACTATAAGACCGACTTCGACAAG
AATAAGATCTGGTATGAGCACCGGCTCATTGATGACATGGTGGCTCAGGTCCTCAAGTCT
TCGGGTGGCTTTGTGTGGGCCTGCAAGAACTATGACGGAGATGTGCAGTCAGACATCCTG
GCCCAGGGCTTTGGCTCCCTTGGCCTGATGACGTCCGTCCTGGTCTGCCCTGATGGGAAG
ACGATTGAGGCTGAGGCCGCTCATGGGACCGTCACCCGCCACTATCGGGAGCACCAGAAG
GGCCGGCCCACCAGCACCAACCCCATCGCCAGCATCTTTGCCTGGACACGTGGCCTGGAG
CACCGGGGGAAGCTGGATGGGAACCAAGACCTCATCAGGTTTGCCCAGATGCTGGAGAAG
GTGTGCGTGGAGACGGTGGAGAGTGGAGCCATGACCAAGGACCTGGCGGGCTGCATTCAC
GGCCTCAGCAATGTGAAGCTGAACGAGCACTTCCTGAACACCATGGACTTCCTCGACACC
ATCAAGAGCAACCTGGACAGAGCCCTGGGCAGGCAGTAG
|
| Enzyme 3 GenBank Gene ID |
X69433  |
| Enzyme 3 GeneCard ID |
IDH2  |
| Enzyme 3 GenAtlas ID |
IDH2  |
| Enzyme 3 HGNC ID |
HGNC:5383  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
15q26.1 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6179 |
| Enzyme 4 Name |
Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial |
| Enzyme 4 Synonyms |
- Isocitric dehydrogenase subunit beta
- NAD(+)-specific ICDH subunit beta
|
| Enzyme 4 Gene Name |
IDH3B |
| Enzyme 4 Protein Sequence |
>Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVG
PELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPME
YKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESAR
GVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELY
PKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEY
AVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRT
RDMGGYSTTTDFIKSVIGHLQTKGS
|
| Enzyme 4 Number of Residues |
385 |
| Enzyme 4 Molecular Weight |
42183.4 |
| Enzyme 4 Theoretical pI |
8.66 |
| Enzyme 4 GO Classification |
| Function |
- NAD or NADH binding
- binding
- catalytic activity
- cation binding
- ion binding
- isocitrate dehydrogenase (NAD+) activity
- isocitrate dehydrogenase activity
- magnesium ion binding
- metal ion binding
- nucleotide binding
- 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 |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- oxidation reduction
- tricarboxylic acid cycle
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 4 General Function |
Involved in magnesium ion binding |
| Enzyme 4 Specific Function |
Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH [RN:R00709]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
28178821  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
O43837  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
IDH3B_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1158 bp
ATGGCGGCATTGAGCGGAGTCCGCTGGCTGACCCGAGCGCTGGTCTCCGCCGGGAACCCT
GGGGCATGGAGAGGTCTGAGTACCTCGGCCGCGGCGCACGCTGCATCGCGGAGCCAGGCC
GAGGACGTGAGGGTGGAGGGCTCCTTTCCCGTGACCATGCTTCCGGGAGACGGTGTGGGG
CCTGAGCTGATGCACGCCGTCAAGGAGGTGTTCAAGGCTGCCGCTGTCCCAGTGGAGTTC
CAGGAGCACCACCTGAGTGAGGTGCAGAATATGGCATCTGAGGAGAAGCTGGAGCAGGTG
CTGAGTTCCATGAAGGAGAACAAAGTGGCCATCATTGGAAAGATTCATACCCCGATGGAG
TATAAGGGGGAGCTAGCCTCCTATGATATGCGGCTGAGGCGTAAGTTGGACTTATTTGCC
AACGTAGTCCATGTGAAGTCACTTCCTGGGTATATGACTCGGCACAACAATCTAGACCTG
GTGATCATTCGAGAGCAGACAGAAGGGGAGTACAGCTCTCTGGAACATGAGAGTGCAAGG
GGTGTGATTGAGTGTTTGAAGATTGTCACACGAGCCAAGTCTCAGCGGATTGCAAAGTTC
GCCTTTGACTATGCCACCAAGAAGGGGCGGGGCAAGGTCACTGCTGTCCACAAGGCCAAC
ATCATGAAACTTGGGGATGGGTTGTTCCTGCAGTGCTGTGAGGAAGTTGCTGAACTGTAC
CCCAAAATCAAATTTGAGACAATGATCATAGACAACTGCTGCATGCAGCTGGTGCAGAAT
CCTTACCAGTTTGATGTGCTTGTGATGCCCAATCTCTATGGGAACATTATTGACAATCTG
GCTGCTGGCCTGGTTGGGGGAGCTGGTGTGGTCCCTGGTGAGAGCTATAGTGCAGAATAC
GCAGTCTTTGAGACGGGTGCCCGGCACCCATTTGCCCAGGCAGTGGGCAGGAATATAGCC
AATCCCACGGCCATGCTGCTGTCGGCTTCCAACATGCTGCGGCATCTTAATCTTGAGTAT
CACTCCAGCATGATCGCAGATGCGGTGAAGAAGGTGATCAAAGTTGGCAAGGTGCGGACT
CGAGACATGGGCGGCTACAGCACCACAACCGACTTCATCAAGTCTGTCATCGGTCACCTG
CAGACTAAAGGGAGCTAG
|
| Enzyme 4 GenBank Gene ID |
NM_006899.2  |
| Enzyme 4 GeneCard ID |
IDH3B  |
| Enzyme 4 GenAtlas ID |
IDH3B  |
| Enzyme 4 HGNC ID |
HGNC:5385  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
20p13 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- 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
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- 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
]
- Hartong DT, Dange M, McGee TL, Berson EL, Dryja TP, Colman RF: Insights from retinitis pigmentosa into the roles of isocitrate dehydrogenases in the Krebs cycle. Nat Genet. 2008 Oct;40(10):1230-4. Epub 2008 Sep 21. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6180 |
| Enzyme 5 Name |
Isocitrate dehydrogenase [NADP] cytoplasmic |
| Enzyme 5 Synonyms |
- IDH
- Cytosolic NADP-isocitrate dehydrogenase
- IDP
- NADP(+)-specific ICDH
- Oxalosuccinate decarboxylase
|
| Enzyme 5 Gene Name |
IDH1 |
| Enzyme 5 Protein Sequence |
>Isocitrate dehydrogenase [NADP] cytoplasmic
MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDA
AEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRL
VSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAM
GMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFE
AQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDG
KTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALE
EVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL
|
| Enzyme 5 Number of Residues |
414 |
| Enzyme 5 Molecular Weight |
46659.0 |
| Enzyme 5 Theoretical pI |
7.00 |
| Enzyme 5 GO Classification |
| Function |
- NAD or NADH binding
- binding
- catalytic activity
- cation binding
- ion binding
- isocitrate dehydrogenase (NADP+) activity
- isocitrate dehydrogenase activity
- magnesium ion binding
- metal ion binding
- nucleotide binding
- 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 |
- carboxylic acid metabolic process
- cellular metabolic process
- isocitrate metabolic process
- metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in magnesium ion binding |
| Enzyme 5 Specific Function |
Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- (1) isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+ (overall reaction) [RN:R00267]
- (2) (1a) isocitrate + NADP+ = oxalosuccinate + NADPH + H+ [RN:R01899]
- (3) (1b) oxalosuccinate = 2-oxoglutarate + CO2 [RN:R00268]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
3641398  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
O75874  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
IDHC_HUMAN  |
| Enzyme 5 PDB ID |
1T0L  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 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 5 GenBank Gene ID |
AF020038  |
| Enzyme 5 GeneCard ID |
IDH1  |
| Enzyme 5 GenAtlas ID |
IDH1  |
| Enzyme 5 HGNC ID |
HGNC:5382  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
2q33.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- 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
]
- 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
]
- 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
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- 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
]
- 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
]
- Xu X, Zhao J, Xu Z, Peng B, Huang Q, Arnold E, Ding J: Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. J Biol Chem. 2004 Aug 6;279(32):33946-57. Epub 2004 Jun 1. [PubMed
]
- Dang L, White DW, Gross S, Bennett BD, Bittinger MA, Driggers EM, Fantin VR, Jang HG, Jin S, Keenan MC, Marks KM, Prins RM, Ward PS, Yen KE, Liau LM, Rabinowitz JD, Cantley LC, Thompson CB, Vander Heiden MG, Su SM: Cancer-associated IDH1 mutations produce 2-hydroxyglutarate. Nature. 2009 Dec 10;462(7274):739-44. Epub . [PubMed
]
- 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
]
- Parsons DW, Jones S, Zhang X, Lin JC, Leary RJ, Angenendt P, Mankoo P, Carter H, Siu IM, Gallia GL, Olivi A, McLendon R, Rasheed BA, Keir S, Nikolskaya T, Nikolsky Y, Busam DA, Tekleab H, Diaz LA Jr, Hartigan J, Smith DR, Strausberg RL, Marie SK, Shinjo SM, Yan H, Riggins GJ, Bigner DD, Karchin R, Papadopoulos N, Parmigiani G, Vogelstein B, Velculescu VE, Kinzler KW: An integrated genomic analysis of human glioblastoma multiforme. Science. 2008 Sep 26;321(5897):1807-12. Epub 2008 Sep 4. [PubMed
]
- Bleeker FE, Lamba S, Leenstra S, Troost D, Hulsebos T, Vandertop WP, Frattini M, Molinari F, Knowles M, Cerrato A, Rodolfo M, Scarpa A, Felicioni L, Buttitta F, Malatesta S, Marchetti A, Bardelli A: IDH1 mutations at residue p.R132 (IDH1(R132)) occur frequently in high-grade gliomas but not in other solid tumors. Hum Mutat. 2009 Jan;30(1):7-11. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6181 |
| Enzyme 6 Name |
Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial |
| Enzyme 6 Synonyms |
- Isocitric dehydrogenase subunit alpha
- NAD(+)-specific ICDH subunit alpha
|
| Enzyme 6 Gene Name |
IDH3A |
| Enzyme 6 Protein Sequence |
>Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAP
IQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDL
YANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIA
EFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAESCKDIKFNEMYLDTVCLNMV
QDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKD
MANPTALLLSAVMMLRHMGLFDHAARIEAACFATIKDGKSLTKDLGGNAKCSDFTEEICR
RVKDLD
|
| Enzyme 6 Number of Residues |
366 |
| Enzyme 6 Molecular Weight |
39591.4 |
| Enzyme 6 Theoretical pI |
6.93 |
| Enzyme 6 GO Classification |
| Function |
- NAD or NADH binding
- binding
- catalytic activity
- cation binding
- ion binding
- isocitrate dehydrogenase (NAD+) activity
- isocitrate dehydrogenase activity
- magnesium ion binding
- metal ion binding
- nucleotide binding
- 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 |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- oxidation reduction
- tricarboxylic acid cycle
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 6 General Function |
Involved in magnesium ion binding |
| Enzyme 6 Specific Function |
Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH [RN:R00709]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P50213  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
IDH3A_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1101 bp
ATGGCTGGGCCCGCGTGGATCTCCAAGGTCTCTCGGCTGCTGGGGGCATTCCACAACCCA
AAACAGGTGACCAGAGGTTTTACTGGTGGTGTTCAGACAGTAACTTTAATTCCAGGAGAT
GGTATTGGCCCAGAAATTTCAGCTGCAGTTATGAAGATTTTTGATGCTGCCAAAGCACCT
ATTCAGTGGGAGGAGCGGAACGTCACTGCCATTCAAGGACCTGGAGGAAAGTGGATGATC
CCTTCAGAGGCTAAAGAGTCCATGGATAAGAACAAGATGGGCTTGAAAGGCCCTTTGAAG
ACCCCAATAGCAGCCGGTCACCCATCTATGAATTTACTGCTGCGCAAAACATTTGACCTT
TACGCGAATGTCCGACCATGTGTCTCTATCGAAGGCTATAAAACCCCTTACACCGATGTA
AATATTGTGACCATTCGAGAGAACACAGAAGGAGAATACAGTGGAATTGAGCATGTGATT
GTTGATGGAGTCGTGCAGAGTATCAAGCTCATCACCGAGGGGGCGAGCAAGCGCATTGCT
GAGTTTGCCTTTGAGTATGCCCGGAACAACCACCGGAGCAACGTCACGGCGGTGCACAAA
GCCAACATCATGCGGATGTCAGATGGGCTTTTTCTACAAAAATGCAGGGAAGTTGCAGAA
AGCTGTAAAGATATTAAATTTAATGAGATGTACCTTGATACAGTATGTTTGAATATGGTA
CAAGATCCTTCCCAATTTGATGTTCTTGTTATGCCAAATTTGTATGGAGACATCCTTAGT
GACTTGTGTGCAGGATTGATCGGAGGTCTCGGTGTGACACCAAGTGGCAACATTGGAGCC
AATGGGGTTGCAATTTTTGAGTCGGTTCATGGGACGGCTCCAGACATTGCAGGCAAGGAC
ATGGCGAATCCCACAGCCCTCCTGCTCAGTGCCGTGATGATGCTGCGCCACATGGGACTT
TTTGACCATGCTGCAAGAATTGAGGCTGCGTGTTTTGCTACAATTAAGGACGGAAAGAGC
TTGACAAAAGATTTGGGAGGCAATGCAAAATGCTCAGACTTCACAGAGGAAATCTGTCGC
CGAGTAAAAGATTTAGATTAA
|
| Enzyme 6 GenBank Gene ID |
U07681  |
| Enzyme 6 GeneCard ID |
IDH3A  |
| Enzyme 6 GenAtlas ID |
IDH3A  |
| Enzyme 6 HGNC ID |
HGNC:5384  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
15q25.1-q25.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- 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
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- 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
]
- 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
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6182 |
| Enzyme 7 Name |
Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial |
| Enzyme 7 Synonyms |
- Isocitric dehydrogenase subunit gamma
- NAD(+)-specific ICDH subunit gamma
|
| Enzyme 7 Gene Name |
IDH3G |
| Enzyme 7 Protein Sequence |
>Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial
MALKVATVAGSAAKAVLGPALLCRPWEVLGAHEVPSRNIFSEQTIPPSAKYGGRHTVTMI
PGDGIGPELMLHVKSVFRHACVPVDFEEVHVSSNADEEDIRNAIMAIRRNRVALKGNIET
NHNLPPSHKSRNNILRTSLDLYANVIHCKSLPGVVTRHKDIDILIVRENTEGEYSSLEHE
SVAGVVESLKIITKAKSLRIAEYAFKLAQESGRKKVTAVHKANIMKLGDGLFLQCCREVA
ARYPQITFENMIVDNTTMQLVSRPQQFDVMVMPNLYGNIVNNVCAGLVGGPGLVAGANYG
HVYAVFETATRNTGKSIANKNIANPTATLLASCMMLDHLKLHSYATSIRKAVLASMDNEN
MHTPDIGGQGTTSEAIQDVIRHIRVINGRAVEA
|
| Enzyme 7 Number of Residues |
393 |
| Enzyme 7 Molecular Weight |
42794.0 |
| Enzyme 7 Theoretical pI |
8.66 |
| Enzyme 7 GO Classification |
| Function |
- NAD or NADH binding
- binding
- catalytic activity
- cation binding
- ion binding
- isocitrate dehydrogenase (NAD+) activity
- isocitrate dehydrogenase activity
- magnesium ion binding
- metal ion binding
- nucleotide binding
- 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 |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- oxidation reduction
- tricarboxylic acid cycle
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- mitochondrion
- organelle
|
|
| Enzyme 7 General Function |
Involved in magnesium ion binding |
| Enzyme 7 Specific Function |
Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH [RN:R00709]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
1167849  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P51553  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
IDH3G_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 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 7 GenBank Gene ID |
Z68907  |
| Enzyme 7 GeneCard ID |
IDH3G  |
| Enzyme 7 GenAtlas ID |
IDH3G  |
| Enzyme 7 HGNC ID |
HGNC:5386  |
| Enzyme 7 Chromosome Location |
Not Available |
| Enzyme 7 Locus |
Not Available |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
16508 |
| Enzyme 8 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 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
IDH3B |
| Enzyme 8 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 8 Number of Residues |
385 |
| Enzyme 8 Molecular Weight |
42184 |
| Enzyme 8 Theoretical pI |
8.66 |
| Enzyme 8 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 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 |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
B2RDR1  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
B2RDR1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
Not Available |
| Enzyme 8 GenBank Gene ID |
AK315641  |
| Enzyme 8 GeneCard ID |
B2RDR1  |
| Enzyme 8 GenAtlas ID |
Not Available |
| Enzyme 8 HGNC ID |
Not Available |
| Enzyme 8 Chromosome Location |
20 |
| Enzyme 8 Locus |
20p13 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
Not Available |
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
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| Enzyme 9 ID |
16509 |
| Enzyme 9 Name |
cDNA, FLJ93011, Homo sapiens isocitrate dehydrogenase 2 (NADP+), mitochondrial(IDH2), mRNA (Isocitrate dehydrogenase 2 (NADP+), mitochondrial, isoform CRA_a) |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
IDH2 |
| Enzyme 9 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
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| Enzyme 9 Number of Residues |
452 |
| Enzyme 9 Molecular Weight |
50910 |
| Enzyme 9 Theoretical pI |
8.95 |
| Enzyme 9 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
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| Process |
- cellular metabolism
- energy derivation by oxidation of organic compounds
- generation of precursor metabolites and energy
- main pathways of carbohydrate metabolism
- metabolism
- physiological process
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| Component |
| — |
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| Enzyme 9 General Function |
Energy production and conversion |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
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| Enzyme 9 Signals |
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| Enzyme 9 Transmembrane Regions |
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| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
B2R6L6  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
B2R6L6_HUMAN  |
| Enzyme 9 PDB ID |
1LWD  |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
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| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
Not Available |
| Enzyme 9 GenBank Gene ID |
AK312627  |
| Enzyme 9 GeneCard ID |
B2R6L6  |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
Not Available |
| Enzyme 9 Chromosome Location |
15 |
| Enzyme 9 Locus |
15q26.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
Not Available |
| Enzyme 9 Metabolite References |
Not Available |