1. (2E)-But-2-enedioate
2. (2E)-But-2-enedioic acid
3. (E)-2-Butenedioate
4. (E)-2-Butenedioic acid
5. 2-(E)-Butenedioate
6. 2-(E)-Butenedioic acid
7. Allomaleate
8. Allomaleic acid
9. Boletate
10. Boletic acid
11. FC 33
12. Fumarate
13. Fumaric acid
14. Lichenate
15. Lichenic acid
16. trans-1,2-Ethylenedicarboxylate
17. trans-1,2-Ethylenedicarboxylic acid
18. trans-2-Butenedioate
19. trans-2-Butenedioic acid
20. trans-Butenedioate
21. trans-Butenedioic acid
22. sodium fumarate

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• Cytoplasm (Predicted from LogP)
• mitochondria

• Blood
• Cerebrospinal Fluid
• Urine

• 104300 (Alzheimer's disease)
• 606812 (Fumarase deficiency)
• 211980 (Lung Cancer)

1. 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 ]
2. 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 ]
3. Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed ]
4. 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 ]
5. Wikipedia

1. Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial precursor
2. Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial precursor
3. Dopamine beta-hydroxylase precursor
4. Adenylosuccinate lyase
5. Argininosuccinate lyase
6. Fumarylacetoacetase
7. Fumarate hydratase, mitochondrial precursor
8. Fumarate hydratase (Fumarate hydratase, isoform CRA_c) (cDNA, FLJ92753, Homo sapiens fumarate hydratase (FH), nuclear gene encodingmitochondrial protein, mRNA)
9. Succinate dehydrogenase complex, subunit C delta5 alternative splicing variant
10. Integral membrane protein CII-3b (Succinate dehydrogenase complex, subunit C, integral membrane protein, 15kDa, isoform CRA_g) (Succinate dehydrogenase complex, subunit C delta3 alternative splicing variant)
11. cDNA, FLJ94596, Homo sapiens fumarylacetoacetate hydrolase (fumarylacetoacetase)(FAH), mRNA (Fumarylacetoacetate hydrolase (Fumarylacetoacetase), isoform CRA_a)
12. cDNA, FLJ92337, highly similar to Homo sapiens succinate dehydrogenase complex, subunit B, iron sulfur (Ip) (SDHB), mRNA (Succinate dehydrogenase complex, subunit B, iron sulfur (Ip), isoform CRA_a)

1. Fp
2. Flavoprotein subunit of complex II

MSGVRGLSRLLSARRLALAKAWPTVLQTGTRGFHFTVDGNKRASAKVSDSISAQYPVVDH
EFDAVVVGAGGAGLRAAFGLSEAGFNTACVTKLFPTRSHTVAAQGGINAALGNMEEDNWR
WHFYDTVKGSDWLGDQDAIHYMTEQAPAAVVELENYGMPFSRTEDGKIYQRAFGGQSLKF
GKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIE
DGSIHRIRAKNTVVATGGYGRTYFSCTSAHTSTGDGTAMITRAGLPCQDLEFVQFHPTGI
YGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPE
KDHVYLQLHHLPPEQLATRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQ
VLRHVNGQDQIVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIEESCRPGDK
VPPIKPNAGEESVMNLDKLRFADGSIRTSELRLSMQKSMQNHAAVFRVGSVLQEGCGKIS
KLYGDLKHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGAHAREDYKVR
IDEYDYSKPIQGQQKKPFEEHWRKHTLSYVDVGTGKVTLEYRPVIDKTLNEADCATVPPA
IRSY

• Citrate Cycle (map00020 )
• Oxidative phosphorylation (map00190 )

• succinate + ubiquinone = fumarate + ubiquinol

• FAD_binding_2 (PF00890 )
• Succ_DH_flav_C (PF02910 )

• 1-19

ATGTCGGGGGTCCGGGGCCTGTCGCGGCTGCTGAGCGCTCGGCGCCTGGCGCTGGCCAAG
GCGTGGCCAACAGTGTTGCAAACAGGAACCCGAGGTTTTCACTTCACTGTTGATGGGAAC
AAGAGGGCATCTGCTAAAGTTTCAGATTCCATTTCTGCTCAGTATCCAGTAGTGGATCAT
GAATTTGATGCAGTGGTGGTAGGCGCTGGAGGGGCAGGCTTGCGAGCTGCATTTGGCCTT
TCTGAGGCAGGGTTTAATACAGCATGTGTTACCAAGCTGTTTCCTACCAGGTCACACACT
GTTGCAGCACAGGGAGGAATCAATGCTGCTCTGGGGAACATGGAGGAGGACAACTGGAGG
TGGCATTTCTACGACACCGTGAAGGGCTCCGACTGGCTGGGGGACCAGGATGCCATCCAC
TACATGACGGAGCAGGCCCCCGCCGCCGTGGTCGAGCTAGAAAATTATGGCATGCCGTTT
AGCAGAACTGAAGATGGGAAGATTTATCAGCGTGCATTTGGTGGACAGAGCCTCAAGTTT
GGAAAGGGCGGGCAGGCCCATCGGTGCTGCTGTGTGGCTGATCGGACTGGCCACTCGCTA
TTGCACACCTTATATGGACGGTCTCTGCGATATGATACCAGCTATTTTGTGGAGTATTTT
GCCTTGGATCTCCTGATGGAGAACGGGGAGTGCCGTGGTGTCATCGCACTGTGCATAGAG
GACGGGTCCATCCATCGCATAAGAGCAAAGAACACTGTTGTTGCCACAGGAGGCTACGGG
CGCACCTACTTCAGCTGCACGTCTGCCCACACCAGCACTGGCGACGGCACGGCCATGATC
ACCAGGGCAGGCCTTCCTTGCCAGGACCTAGAGTTTGTTCAGTTCCACCCTACAGGCATA
TATGGTGCTGGTTGTCTCATTACGGAAGGATGTCGTGGAGAGGGAGGCATTCTCATTAAC
AGTCAAGGCGAAAGGTTTATGGAGCGATACGCCCCTGTCGCGAAGGACCTGGCGTCTAGA
GATGTGGTGTCTCGGTCCATGACTCTGGAGATCCGAGAAGGAAGAGGCTGTGGCCCTGAG
AAAGATCACGTCTACCTGCAGCTGCACCACCTACCTCCAGAGCAGCTGGCCACGCGCCTG
CCTGGCATTTCAGAGACAGCCATGATCTTCGCTGGCGTGGACGTCACGAAGGAGCCGATC
CCTGTCCTCCCCACCGTGCATTATAACATGGGCGGCATTCCCACCAACTACAAGGGGCAG
GTCCTGAGGCACGTGAATGGCCAGGATCAGATTGTGCCCGGCCTGTACGCCTGTGGGGAG
GCCGCCTGTGCCTCGGTACATGGTGCCAACCGCCTCGGGGCAAACTCGCTCTTGGACCTG
GTTGTCTTTGGTCGGGCATGTGCCCTGAGCATCGAAGAGTCATGCAGGCCTGGAGATAAA
GTCCCTCCAATTAAACCAAACGCTGGGGAAGAATCTGTCATGAATCTTGACAAATTGAGA
TTTGCTGATGGAAGCATAAGAACATCGGAACTGCGACTCAGCATGCAGAAGTCAATGCAA
AATCATGCTGCCGTGTTCCGTGTGGGAAGCGTGTTGCAAGAAGGTTGTGGGAAAATCAGC
AAGCTCTATGGAGACCTAAAGCACCTGAAGACGTTCGACCGGGGAATGGTCTGGAACACG
GACCTGGTGGAGACCCTGGAGCTGCAGAACCTGATGCTGTGTGCGCTGCAGACCATCTAC
GGAGCAGAGGCACGGAAGGAGTCACGGGGCGCGCATGCCAGGGAAGACTACAAGGTGCGG
ATTGATGAGTACGATTACTCCAAGCCCATCCAGGGGCAACAGAAGAAGCCCTTTGAGGAG
CACTGGAGGAAGCACACCCTGTCCTATGTGGACGTTGGCACTGGGAAGGTCACTCTGGAA
TATAGACCCGTGATCGACAAAACTTTGAACGAGGCTGACTGTGCCACCGTCCCGCCAGCC
ATTCGCTCCTACTGA

1. Hirawake H, Wang H, Kuramochi T, Kojima S, Kita K: Human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the flavoprotein (Fp) subunit of liver mitochondria. J Biochem (Tokyo). 1994 Jul;116(1):221-7. [PubMed ]
2. Morris AA, Farnsworth L, Ackrell BA, Turnbull DM, Birch-Machin MA: The cDNA sequence of the flavoprotein subunit of human heart succinate dehydrogenase. Biochim Biophys Acta. 1994 Mar 29;1185(1):125-8. [PubMed ]
3. Bourgeron T, Rustin P, Chretien D, Birch-Machin M, Bourgeois M, Viegas-Pequignot E, Munnich A, Rotig A: Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency. Nat Genet. 1995 Oct;11(2):144-9. [PubMed ]
4. Van Coster R, Seneca S, Smet J, Van Hecke R, Gerlo E, Devreese B, Van Beeumen J, Leroy JG, De Meirleir L, Lissens W: Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II. Am J Med Genet A. 2003 Jul 1;120(1):13-8. [PubMed ]

1. CybS
2. Succinate-ubiquinone reductase membrane anchor subunit
3. QPs3
4. CII-4
5. Succinate dehydrogenase complex subunit D
6. Succinate-ubiquinone oxidoreductase cytochrome b small subunit

MAVLWRLSAVCGALGGRALLLRTPVVRPAHISAFLQDRPIPEWCGVQHIHLSPSHHSGSK
AASLHWTSERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGLGQVVTDYVHGDAL
QKAAKAGLLALSALTFAGLCYFNYHDVGICKAVAMLWKL

• CybS (PF05328 )

• 1-18

• 71-91 126-142

ATGGCGGTTCTCTGGAGGCTGAGTGCCGTTTGCGGTGCCCTAGGAGGCCGAGCTCTGTTG
CTTCGAACTCCAGTGGTCAGACCTGCTCATATCTCAGCATTTCTTCAGGACCGACCTATC
CCAGAATGGTGTGGAGTGCAGCACATACACTTGTCACCGAGCCACCATTCTGGCTCCAAG
GCTGCATCTCTCCACTGGACTAGCGAGAGGGTTGTCAGTGTTTTGCTCCTGGGTCTGCTT
CCGGCTGCTTATTTGAATCCTTGCTCTGCGATGGACTATTCCCTGGCTGCAGCCCTCACT
CTTCATGGTCACTGGGGCCTTGGACAAGTTGTTACTGACTATGTTCATGGGGATGCCTTG
CAGAAAGCTGCCAAGGCAGGGCTTTTGGCACTTTCAGCTTTAACCTTTGCTGGGCTTTGC
TATTTCAACTATCACGATGTGGGCATCTGCAAAGCTGTTGCCATGCTGTGGAAGCTCTGA

1. Hirawake H, Taniwaki M, Tamura A, Kojima S, Kita K: Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase): cDNA cloning of the components in liver mitochondria and chromosome assignment of the genes for the large (SDHC) and small (SDHD) subunits to 1q21 and 11q23. Cytogenet Cell Genet. 1997;79(1-2):132-8. [PubMed ]
2. Gimm O, Armanios M, Dziema H, Neumann HP, Eng C: Somatic and occult germ-line mutations in SDHD, a mitochondrial complex II gene, in nonfamilial pheochromocytoma. Cancer Res. 2000 Dec 15;60(24):6822-5. [PubMed ]
3. Baysal BE, Ferrell RE, Willett-Brozick JE, Lawrence EC, Myssiorek D, Bosch A, van der Mey A, Taschner PE, Rubinstein WS, Myers EN, Richard CW 3rd, Cornelisse CJ, Devilee P, Devlin B: Mutations in SDHD, a mitochondrial complex II gene, in hereditary paraganglioma. Science. 2000 Feb 4;287(5454):848-51. [PubMed ]
4. Milunsky JM, Maher TA, Michels VV, Milunsky A: Novel mutations and the emergence of a common mutation in the SDHD gene causing familial paraganglioma. Am J Med Genet. 2001 May 15;100(4):311-4. [PubMed ]
5. Badenhop RF, Cherian S, Lord RS, Baysal BE, Taschner PE, Schofield PR: Novel mutations in the SDHD gene in pedigrees with familial carotid body paraganglioma and sensorineural hearing loss. Genes Chromosomes Cancer. 2001 Jul;31(3):255-63. [PubMed ]
6. Taschner PE, Jansen JC, Baysal BE, Bosch A, Rosenberg EH, Brocker-Vriends AH, van Der Mey AG, van Ommen GJ, Cornelisse CJ, Devilee P: Nearly all hereditary paragangliomas in the Netherlands are caused by two founder mutations in the SDHD gene. Genes Chromosomes Cancer. 2001 Jul;31(3):274-81. [PubMed ]
7. Masuoka J, Brandner S, Paulus W, Soffer D, Vital A, Chimelli L, Jouvet A, Yonekawa Y, Kleihues P, Ohgaki H: Germline SDHD mutation in paraganglioma of the spinal cord. Oncogene. 2001 Aug 16;20(36):5084-6. [PubMed ]
8. Kytola S, Nord B, Elder EE, Carling T, Kjellman M, Cedermark B, Juhlin C, Hoog A, Isola J, Larsson C: Alterations of the SDHD gene locus in midgut carcinoids, Merkel cell carcinomas, pheochromocytomas, and abdominal paragangliomas. Genes Chromosomes Cancer. 2002 Jul;34(3):325-32. [PubMed ]
9. Cascon A, Ruiz-Llorente S, Cebrian A, Leton R, Telleria D, Benitez J, Robledo M: G12S and H50R variations are polymorphisms in the SDHD gene. Genes Chromosomes Cancer. 2003 Jun;37(2):220-1. [PubMed ]

1. Dopamine beta- monooxygenase

MREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLELSWNVSYTQEAIHF
QLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQKGQIHLDPQQDYQLL
QVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSLEAINGSGLQMGLQR
VQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEPIVT
KGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLAAWALGAKAFYYPEE
AGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPV
MAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKVVTVLVRDGREWEIV
NQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHY
YPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFTSVPWNSFNRDVLKA
LYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQGRSPAGPTVVSIGG
GKG

• Tyrosine Metabolism (map00350 )

• 3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O

• Cu2_monoox_C (PF03712 )
• Cu2_monooxygen (PF01082 )
• DOMON (PF03351 )

• 1-25

ATGCGGGAGGCAGCCTTCATGTACAGCACAGCAGTGGCCATCTTCCTGGTCATCCTGGTG
GCCGCACTGCAGGGCTCGGCTCCCCGTGAGAGCCCCCTCCCCTATCACATCCCCCTGGAC
CCGGAGGGGTCCCTGGAGCTCTCATGGAATGTCAGCTACACCCAGGAGGCCATCCATTTC
CAGCTCCTGGTGCGGAGGCTCAAGGCTGGCGTCCTGTTTGGGATGTCCGACCGTGGCGAG
CTTGAGAACGCAGATCTCGTGGTGCTCTGGACCGATGGGGACACTGCCTATTTTGCGGAC
GCCTGGAGTGACCAGAAGGGGCAGATCCACCTGGATCCCCAGCAGGACTACCAGCTGCTG
CAGGTGCAGAGGACCCCAGAAGGCCTGACCCTGCTTTTCAAGAGGCCCTTTGGCACCTGC
GACCCCAAGGATTACCTCATTGAAGACGGCACTGTCCACTTGGTCTACGGGATCCTGGAG
GAGCCGTTCCGGTCACTGGAGGCCATCAACGGCTCGGGCCTGCAGATGGGGCTGCAGAGG
GTGCAGCTCCTGAAGCCCAATATCCCCGAACCGGAGTTGCCCTCAGACGCGTGCACCATG
GAGGTCCAAGCTCCCAATATCCAGATCCCCAGCCAGGAGACCACGTACTGGTGCTACATT
AAGGAGCTTCCAAAGGGCTTCTCTCGGCACCACATTATCAAGTACGAGCCCATCGTCACC
AAGGGCAATGAGGCCCTTGTCCACCACATGGAAGTCTTCCAGTGCGCCCCCGAGATGGAC
AGCGTCCCCCACTTCAGCGGGCCCTGCGACTCCAAGATGAAACCCGACCGCCTCAACTAC
TGCCGCCACGTGCTGGCCGCCTGGGCCCTGGGTGCCAAGGCATTTTACTACCCAGAGGAA
GCCGGCCTTGCCTTCGGGGGTCCAGGGTCCTCCAGATATCTCCGCCTGGAAGTTCACTAC
CACAACCCACTGGTGATAGAAGGACGAAACGACTCCTCAGGCATCCGCTTGTACTACACA
GCCAAGCTGCGGCGCTTCAACGCGGGGATCATGGAGCTGGGACTGGTGTACACGCCAGTG
ATGGCCATTCCACCACGGGAGACCGCCTTCATCCTCACTGGCTACTGCACGGACAAGTGC
ACCCAGCTGGCACTGCCTCCCTCCGGGATCCACATCTTCGCCTCTCAGCTCCACACACAC
CTGACTGGGAGAAAGGTGGTCACAGTGCTGGTCCGGGACGGCCGGGAGTGGGAGATCGTG
AACCAGGACAATCACTACAGCCCTCACTTCCAGGAGATCCGCATGTTGAAGAAGGTCGTG
TCGGTCCATCCGGGAGATGTGCTCATCACCTCCTGCACGTACAACACGGAAGACCGGGAG
CTGGCCACAGTGGGGGGCTTCGGGATCCTGGAGGAGATGTGTGTCAACTACGTGCACTAC
TACCCCCAGACGCAGCTGGAGCTCTGCAAGACGGCTGTGGACGCCGGCTTCCTGCAGAAG
TACTTCCACCTCATCAACAGGTTCAACAACGAGGATGTCTGCACCTGCCCTCAGGCGTCC
GTGTCTCAGCAGTTCACCTCTGTTCCCTGGAACTCCTTCAACCGCGACGTACTGAAGGCC
CTGTACAGCTTCGCGCCCATCTCCATGCACTGCAACAAGTCCTCAGCCGTCCGCTTCCAG
GGTGAATGGAACCTGCAGCCCCTGCCCAAGGTCATCTCCACACTGGAAGAGCCCACCCCA
CAGTGCCCCACCAGCCAGGGCCGAAGCCCTGCTGGCCCCACCGTTGTCAGCATTGGTGGG
GGCAAAGGCTGA

1. Kobayashi K, Kurosawa Y, Fujita K, Nagatsu T: Human dopamine beta-hydroxylase gene: two mRNA types having different 3'-terminal regions are produced through alternative polyadenylation. Nucleic Acids Res. 1989 Feb 11;17(3):1089-102. [PubMed ]
2. Lamouroux A, Vigny A, Faucon Biguet N, Darmon MC, Franck R, Henry JP, Mallet J: The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme. EMBO J. 1987 Dec 20;6(13):3931-7. [PubMed ]
3. Li B, Tsing S, Kosaka AH, Nguyen B, Osen EG, Bach C, Chan H, Barnett J: Expression of human dopamine beta-hydroxylase in Drosophila Schneider 2 cells. Biochem J. 1996 Jan 1;313 ( Pt 1):57-64. [PubMed ]
4. Williams HJ, Bray N, Murphy KC, Cardno AG, Jones LA, Owen MJ: No evidence for allelic association between schizophrenia and a functional variant of the human dopamine beta-hydroxylase gene (DBH). Am J Med Genet. 1999 Oct 15;88(5):557-9. [PubMed ]
5. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]
6. Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed ]
7. Kim CH, Zabetian CP, Cubells JF, Cho S, Biaggioni I, Cohen BM, Robertson D, Kim KS: Mutations in the dopamine beta-hydroxylase gene are associated with human norepinephrine deficiency. Am J Med Genet. 2002 Mar 1;108(2):140-7. [PubMed ]

1. Adenylosuccinase
2. ASL
3. ASASE

MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDE
QIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTD
LIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLC
MDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITG
QTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMR
SERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISE
GLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGD
NDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKA
ELCL

• Purine Metabolism (map00230 )

• (1) N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP
• (2) (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

• Lyase_1 (PF00206 )

• None

• None

ATGGCGGCTGGAGGCGATCATGGTTCGCCCGACAGCTACCGCTCACCTCTTGCCTCCCGC
TATGCCAGCCCGGAGATGTGCTTCGTGTTTAGCGACAGGTATAAATTCCGGACATGGCGG
CAGCTGTGGCTGTGGCTGGCGGAGGCCGAGCAGACATTGGGTTTGCCTATCACAGATGAA
CAAATCCAGGAGATGAAATCAAACCTGGAGAACATAGACTTCAAGATGGCAGCTGAGGAA
GAGAAACGTTTACGACATGATGTGATGGCTCACGTGCACACATTTGGCCACTGCTGTCCA
AAAGCTGCAGGCATTATTCACCTTGGTGCTACTTCTTGCTATGTTGGAGACAATACTGAC
TTGATTATTCTTAGAAATGCACTTGACCTGCTTTTGCCAAAGCTTGCCAGAGTGATCTCT
CGGCTTGCCGACTTTGCTAAGGAACGAGCCAGTCTACCCACATTAGGTTTCACACATTTC
CAGCCTGCACAGCTGACCACAGTTGGGAAACGTTGCTGTCTTTGGATTCAGGATCTTTGC
ATGGATCTCCAGAACTTGAAGCGTGTCCGAGATGACCTGCGCTTCCGGGGAGTAAAGGGT
ACCACTGGCACTCAGGCCAGTTTCCTGCAGCTCTTTGAGGGAGATGACCATAAGGTAGAG
CAGCTTGACAAGATGGTGACAGAAAAGGCAGGATTTAAGAGAGCTTTCATCATCACAGGG
CAGACATATACACGAAAAGTGGATATTGAAGTACTGTCTGTGCTGGCTAGCTTGGGGGCA
TCAGTGCACAAGATTTGCACCGACATACGCCTCCTGGCAAACCTCAAGGAGATGGAGGAA
CCCTTTGAAAAACAGCAGATTGGCTCAAGTGCGATGCCATATAAGCGGAATCCCATGCGT
TCAGAACGTTGCTGCAGTCTTGCCCGCCACCTGATGACCCTTGTCATGGACCCGCTACAG
ACAGCATCTGTCCAGTGGTTTGAACGCACACTGGATGATAGTGCCAACCGACGGATCTGT
TTGGCCGAGGCATTTCTTACCGCAGATACTATATTGAATACGCTGCAGAACATTTCTGAA
GGATTGGTCGTGTACCCCAAAGTAATTGAACGGCGCATTCGGCAAGAGCTGCCTTTCATG
GCCACAGAGAACATCATCATGGCCATGGTCAAAGCTGGAGGTAGCCGCCAGGATTGCCAT
GAGAAAATCAGAGTGCTTTCTCAGCAGGCAGCTTCTGTGGTTAAGCAGGAAGGGGGTGAC
AATGACCTCATAGAGCGTATCCAGGTTGATGCCTACTTCAGTCCCATTCACTCCCAGTTG
GATCATTTACTGGATCCTTCTTCTTTCACTGGTCGTGCCTCCCAGCAGGTGCAGAGATTC
TTAGAAGAGGAGGTGTATCCCCTGTTAAAACCATATGAAAGCGTGATGAAGGTGAAAGCA
GAATTATGTCTGTAG

1. Kmoch S, Hartmannova H, Stiburkova B, Krijt J, Zikanova M, Sebesta I: Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients. Hum Mol Genet. 2000 Jun 12;9(10):1501-13. [PubMed ]
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 ]
3. Stone RL, Aimi J, Barshop BA, Jaeken J, Van den Berghe G, Zalkin H, Dixon JE: A mutation in adenylosuccinate lyase associated with mental retardation and autistic features. Nat Genet. 1992 Apr;1(1):59-63. [PubMed ]
4. Verginelli D, Luckow B, Crifo C, Salerno C, Gross M: Identification of new mutations in the adenylosuccinate lyase gene associated with impaired enzyme activity in lymphocytes and red blood cells. Biochim Biophys Acta. 1998 Feb 27;1406(1):81-4. [PubMed ]
5. Marie S, Cuppens H, Heuterspreute M, Jaspers M, Tola EZ, Gu XX, Legius E, Vincent MF, Jaeken J, Cassiman JJ, Van den Berghe G: Mutation analysis in adenylosuccinate lyase deficiency: eight novel mutations in the re-evaluated full ADSL coding sequence. Hum Mutat. 1999;13(3):197-202. [PubMed ]
6. Race V, Marie S, Vincent MF, Van den Berghe G: Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency. Hum Mol Genet. 2000 Sep 1;9(14):2159-65. [PubMed ]
7. Castro M, Perez-Cerda C, Merinero B, Garcia MJ, Bernar J, Gil Nagel A, Torres J, Bermudez M, Garavito P, Marie S, Vincent F, Van den Berghe G, Ugarte M: Screening for adenylosuccinate lyase deficiency: clinical, biochemical and molecular findings in four patients. Neuropediatrics. 2002 Aug;33(4):186-9. [PubMed ]

1. Arginosuccinase
2. ASAL

MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEM
DQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTD
LRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVAL
TRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA
EFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKA
GRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENM
GQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLF
SGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA

• Arginine and Proline Metabolism (map00330 )

• (N(omega)-L-arginino)succinate = fumarate + L-arginine

• Lyase_1 (PF00206 )

• None

• None

ATGGCCTCGGAGAGTGGGAAGCTTTGGGGTGGCCGGTTTGTGGGTGCAGTGGACCCCATC
ATGGAGAAGTTCAACGCGTCCATTGCCTACGACCGGCACCTTTGGGAGGTGGATGTTCAA
GGCAGCAAAGCCTACAGCAGGGGCCTGGAGAAGGCAGGGCTCCTCACCAAGGCCGAGATG
GACCAGATACTCCATGGCCTAGACAAGGTGGCTGAGGAGTGGGCCCAGGGCACCTTCAAA
CTGAACTCCAATGATGAGGACATCCACACAGCCAATGAGCGCCGCCTGAAGGAGCTCATT
GGTGCAACGGCAGGGAAGCTGCACACGGGACGGAGCCGGAATGACCAGGTGGTCACAGAC
CTCAGGCTGTGGATGCGGCAGACCTGCTCCACGCTCTCGGGCCTCCTCTGGGAGCTCATT
AGGACCATGGTGGATCGGGCAGAGGCGGAACGTGATGTTCTCTTCCCGGGGTACACCCAT
TTGCAGAGGGCCCAGCCCATCCGCTGGAGCCACTGGATTCTGAGCCACGCCGTGGCACTG
ACCCGAGACTCTGAGCGGCTGCTGGAGGTGCGGAAGCGGATCAATGTCCTGCCCCTGGGG
AGTGGGGCCATTGCAGGCAATCCCCTGGGTGTGGACCGAGAGCTGCTCCGAGCAGAACTC
AACTTTGGGGCCATCACTCTCAACAGCATGGATGCCACTAGTGAGCGGGACTTTGTGGCC
GAGTTCCTGTTCTGGCGTTCGCTGTGCATGACCCATCTCAGCAGGATGGCCGAGGACCTC
ATCCTCTACTGCACCAAGGAATTCAGCTTCGTGCAGCTCTCAGATGCCTACAGCACGGGA
AGCAGCCTGATGCCCCAGAAGAAAAACCCCGACAGTTTGGAGCTGATCCGGAGCAAGGCT
GGGCGTGTGTTTGGGCGGTGTGCCGGGCTCCTGATGACCCTCAAGGGACTTCCCAGCACC
TACAACAAAGACTTACAGGAGGACAAGGAAGCTGTGTTTGAAGTGTCAGACACTATGAGT
GCCGTGCTCCAGGTGGCCACTGGCGTCATCTCTACGCTGCAGATTCACCAAGAGAACATG
GGACAGGCTCTCAGCCCCGACATGCTGGCCACTGACCTTGCCTATTACCTGGTCCGCAAA
GGGATGCCATTCCGCCAGGCCCATGAGGCCTCCGGGAAAGCTGTGTTCATGGCCGAGACC
AAGGGGGTCGCCCTCAACCAGCTGTCACTGCAGGAGCTGCAGACCATCAGCCCCCTGTTC
TCGGGCGACGTGATCTGCGTGTGGGACTACCGGCACAGTGTGGAGCAGTATGGTGCCCTG
GGCGGCACTGCGCGCTCCAGCGTCGACTGGCAAATCCGCCAGGTGCGGGCGCTACTGCAG
GCACAGCAGGCCTAG

1. Matuo S, Tatsuno M, Kobayashi K, Saheki T, Miyata T, Iwanaga S, Amaya Y, Mori M: Isolation of cDNA clones of human argininosuccinate lyase and corrected amino acid sequence. FEBS Lett. 1988 Jul 18;234(2):395-9. [PubMed ]
2. O'Brien WE, McInnes R, Kalumuck K, Adcock M: Cloning and sequence analysis of cDNA for human argininosuccinate lyase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7211-5. [PubMed ]
3. Todd S, McGill JR, McCombs JL, Moore CM, Weider I, Naylor SL: cDNA sequence, interspecies comparison, and gene mapping analysis of argininosuccinate lyase. Genomics. 1989 Jan;4(1):53-9. [PubMed ]
4. Turner MA, Simpson A, McInnes RR, Howell PL: Human argininosuccinate lyase: a structural basis for intragenic complementation. Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9063-8. [PubMed ]
5. Sampaleanu LM, Vallee F, Thompson GD, Howell PL: Three-dimensional structure of the argininosuccinate lyase frequently complementing allele Q286R. Biochemistry. 2001 Dec 25;40(51):15570-80. [PubMed ]
6. Barbosa P, Cialkowski M, O'Brien WE: Analysis of naturally occurring and site-directed mutations in the argininosuccinate lyase gene. J Biol Chem. 1991 Mar 15;266(8):5286-90. [PubMed ]
7. Walker DC, McCloskey DA, Simard LR, McInnes RR: Molecular analysis of human argininosuccinate lyase: mutant characterization and alternative splicing of the coding region. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9625-9. [PubMed ]
8. Kleijer WJ, Garritsen VH, Linnebank M, Mooyer P, Huijmans JG, Mustonen A, Simola KO, Arslan-Kirchner M, Battini R, Briones P, Cardo E, Mandel H, Tschiedel E, Wanders RJ, Koch HG: Clinical, enzymatic, and molecular genetic characterization of a biochemical variant type of argininosuccinic aciduria: prenatal and postnatal diagnosis in five unrelated families. J Inherit Metab Dis. 2002 Sep;25(5):399-410. [PubMed ]

1. Fumarylacetoacetate hydrolase
2. Beta-diketonase
3. FAA

MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQD
VFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPAT
IGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQM
KPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQ
KWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLS
VNLKGEGMSQAATICKSNFKYMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGPEPENFG
SMLELSWKGTKPIDLGNGQTRKFLLDGDEVIITGYCQGDGYRIGFGQCAGKVLPALLPS

• Styrene Degradation (map00643 )
• Tyrosine Metabolism (map00350 )

• 4-fumarylacetoacetate + H2O = acetoacetate + fumarate

• DUF1969 (PF09298 )
• FAA_hydrolase (PF01557 )

• None

• None

ATGTCCTTCATCCCGGTGGCCGAGGATTCCGACTTCCCCATCCACAACCTGCCCTACGGC
GTCTTCTCGACCAGAGGCGACCCAAGACCGAGGATAGGTGTGGCCATTGGCGACCAGATC
CTGGACCTCAGCATCATCAAGCACCTCTTTACTGGTCCTGTCCTCTCCAAACACCAGGAT
GTCTTCAATCAGCCTACACTCAACAGCTTCATGGGCCTGGGTCAGGCTGCCTGGAAGGAG
GCGAGAGTGTTCTTGCAGAACTTGCTGTCTGTGAGCCAAGCCAGGCTCAGAGATGACACC
GAACTTCGGAAGTGTGCATTCATCTCCCAGGCTTCTGCCACGATGCACCTTCCAGCCACC
ATAGGAGACTACACAGACTTCTATTCCTCTCGGCAGCATGCTACCAACGTCGGAATCATG
TTCAGGGACAAGGAGAATGCGTTGATGCCAAATTGGCTGCACTTACCAGTGGGCTACCAT
GGCCGTGCCTCCTCTGTCGTGGTGTCTGGCACCCCAATCCGAAGGCCCATGGGACAGATG
AAACCTGATGACTCTAAGCCTCCCGTATATGGTGCCTGCAAGCTCTTGGACATGGAGCTG
GAAATGGCTTTTTTTGTAGGCCCTGGAAACAGATTGGGAGAGCCGATCCCCATTTCCAAG
GCCCATGAGCACATTTTTGGAATGGTCCTTATGAACGACTGGAGTGCACGAGACATTCAG
AAGTGGGAGTATGTCCCTCTCGGGCCATTCCTTGGGAAGAGTTTTGGGACCACTGTCTCT
CCGTGGGTGGTGCCCATGGATGCTCTCATGCCCTTTGCTGTGCCCAACCCGAAGCAGGAC
CCCAGGCCCCTGCCGTATCTGTGCCATGACGAGCCCTACACATTTGACATCAACCTCTCT
GTTAACCTGAAAGGAGAAGGAATGAGCCAGGCGGCTACCATATGCAAGTCCAATTTTAAG
TACATGTACTGGACGATGCTGCAGCAGCTCACTCACCACTCTGTCAACGGCTGCAACCTG
CGGCCGGGGGACCTCCTGGCTTCTGGGACCATCAGCGGGCCGGAGCCAGAAAACTTCGGC
TCCATGTTGGAACTGTCGTGGAAGGGAACGAAGCCCATAGACCTGGGGAATGGTCAGACC
AGGAAGTTTCTGCTGGACGGGGATGAAGTCATCATAACAGGGTACTGCCAGGGGGATGGT
TACCGCATCGGCTTTGGCCAGTGTGCTGGAAAAGTGCTGCCTGCTCTCCTGCCATCATGA

1. Phaneuf D, Labelle Y, Berube D, Arden K, Cavenee W, Gagne R, Tanguay RM: Cloning and expression of the cDNA encoding human fumarylacetoacetate hydrolase, the enzyme deficient in hereditary tyrosinemia: assignment of the gene to chromosome 15. Am J Hum Genet. 1991 Mar;48(3):525-35. [PubMed ]
2. Agsteribbe E, van Faassen H, Hartog MV, Reversma T, Taanman JW, Pannekoek H, Evers RF, Welling GM, Berger R: Nucleotide sequence of cDNA encoding human fumarylacetoacetase. Nucleic Acids Res. 1990 Apr 11;18(7):1887. [PubMed ]
3. Bergeron A, D'Astous M, Timm DE, Tanguay RM: Structural and functional analysis of missense mutations in fumarylacetoacetate hydrolase, the gene deficient in hereditary tyrosinemia type 1. J Biol Chem. 2001 May 4;276(18):15225-31. Epub 2001 Jan 22. [PubMed ]
4. St-Louis M, Tanguay RM: Mutations in the fumarylacetoacetate hydrolase gene causing hereditary tyrosinemia type I: overview. Hum Mutat. 1997;9(4):291-9. [PubMed ]
5. Phaneuf D, Lambert M, Laframboise R, Mitchell G, Lettre F, Tanguay RM: Type 1 hereditary tyrosinemia. Evidence for molecular heterogeneity and identification of a causal mutation in a French Canadian patient. J Clin Invest. 1992 Oct;90(4):1185-92. [PubMed ]
6. Labelle Y, Phaneuf D, Leclerc B, Tanguay RM: Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity. Hum Mol Genet. 1993 Jul;2(7):941-6. [PubMed ]
7. Grompe M, al-Dhalimy M: Mutations of the fumarylacetoacetate hydrolase gene in four patients with tyrosinemia, type I. Hum Mutat. 1993;2(2):85-93. [PubMed ]
8. Rootwelt H, Berger R, Gray G, Kelly DA, Coskun T, Kvittingen EA: Novel splice, missense, and nonsense mutations in the fumarylacetoacetase gene causing tyrosinemia type 1. Am J Hum Genet. 1994 Oct;55(4):653-8. [PubMed ]
9. Rootwelt H, Brodtkorb E, Kvittingen EA: Identification of a frequent pseudodeficiency mutation in the fumarylacetoacetase gene, with implications for diagnosis of tyrosinemia type I. Am J Hum Genet. 1994 Dec;55(6):1122-7. [PubMed ]
10. Rootwelt H, Chou J, Gahl WA, Berger R, Coskun T, Brodtkorb E, Kvittingen EA: Two missense mutations causing tyrosinemia type 1 with presence and absence of immunoreactive fumarylacetoacetase. Hum Genet. 1994 Jun;93(6):615-9. [PubMed ]
11. St-Louis M, Poudrier J, Phaneuf D, Leclerc B, Laframboise R, Tanguay RM: Two novel mutations involved in hereditary tyrosinemia type I. Hum Mol Genet. 1995 Feb;4(2):319-20. [PubMed ]
12. Hahn SH, Krasnewich D, Brantly M, Kvittingen EA, Gahl WA: Heterozygosity for an exon 12 splicing mutation and a W234G missense mutation in an American child with chronic tyrosinemia type 1. Hum Mutat. 1995;6(1):66-73. [PubMed ]
13. Ploos van Amstel JK, Bergman AJ, van Beurden EA, Roijers JF, Peelen T, van den Berg IE, Poll-The BT, Kvittingen EA, Berger R: Hereditary tyrosinemia type 1: novel missense, nonsense and splice consensus mutations in the human fumarylacetoacetate hydrolase gene; variability of the genotype-phenotype relationship. Hum Genet. 1996 Jan;97(1):51-9. [PubMed ]
14. Bergman AJ, van den Berg IE, Brink W, Poll-The BT, Ploos van Amstel JK, Berger R: Spectrum of mutations in the fumarylacetoacetate hydrolase gene of tyrosinemia type 1 patients in northwestern Europe and Mediterranean countries. Hum Mutat. 1998;12(1):19-26. [PubMed ]

1. Fumarase

MYRALRLLARSRPLVRAPAAALASAPGLGGAAVPSFWPPNAARMASQNSFRIEYDTFGEL
KVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYGLDPKIANAI
MKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDH
VNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAV
PLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL
TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPE
NEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSA
RLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGS
TLKETAIELGYLTAEQFDEWVKPKDMLGPK

• Citrate Cycle (map00020 )

• (S)-malate = fumarate + H2O

• Lyase_1 (PF00206 )

• 1-23

ATGTACCGAGCACTTCGGCTCCTCGCGCGCTCGCGTCCCCTCGTGCGGGCTCCAGCCGCA
GCCTTAGCTTCGGCTCCCGGCTTGGGTGGCGCGGCCGTGCCCTCGTTTTGGCCTCCGAAC
GCGGCTCGAATGGCAAGCCAAAATTCCTTCCGGATAGAATATGATACCTTTGGTGAACTA
AAGGTGCCAAATGATAAGTATTATGGCGCCCAGACCGTGAGATCTACGATGAACTTTAAG
ATTGGAGGTGTGACAGAACGCATGCCAACCCCAGTTATTAAAGCTTTTGGCATCTTGAAG
CGAGCGGCCGCTGAAGTAAACCAGGATTATGGTCTTGATCCAAAGATTGCTAATGCAATA
ATGAAGGCAGCAGATGAGGTAGCTGAAGGTAAATTAAATGATCATTTTCCTCTCGTGGTA
TGGCAGACTGGATCAGGAACTCAGACAAATATGAATGTAAATGAAGTCATTAGCAATAGA
GCAATTGAAATGTTAGGAGGTGAACTTGGCAGCAAGATACCTGTGCATCCCAACGATCAT
GTTAATAAAAGCCAGAGCTCAAATGATACTTTTCCCACAGCAATGCACATTGCTGCTGCA
ATAGAAGTTCATGAAGTACTGTTACCAGGACTACAGAAGTTACATGATGCTCTTGATGCA
AAATCCAAAGAGTTTGCACAGATCATCAAGATTGGACGTACTCATACTCAGGATGCTGTT
CCACTTACTCTTGGGCAGGAATTTAGTGGTTATGTTCAACAAGTAAAATATGCAATGACA
AGAATAAAAGCTGCCATGCCAAGAATCTATGAGCTCGCAGCTGGAGGCACTGCTGTTGGT
ACAGGTTTAAATACTAGAATTGGCTTTGCAGAAAAGGTTGCTGCAAAAGTGGCTGCACTT
ACAGGCTTGCCTTTTGTCACTGCTCCGAATAAATTTGAAGCTCTGGCTGCTCATGACGCT
CTGGTTGAGCTCAGTGGAGCCATGAACACTACTGCCTGCAGTCTGATGAAGATAGCAAAT
GATATTCGATTTTTGGGTTCTGGTCCTCGGTCAGGTCTGGGAGAATTGATCTTGCCTGAA
AATGAACCAGGAAGCAGTATCATGCCAGGCAAGGTGAACCCTACTCAGTGTGAAGCAATG
ACCATGGTTGCAGCCCAAGTCATGGGGAACCATGTTGCTGTCACTGTCGGAGGCAGCAAT
GGACATTTTGAGTTGAATGTTTTCAAGCCAATGATGATTAAAAATGTGTTACACTCAGCC
AGGCTGCTGGGGGATGCTTCAGTTTCCTTTACAGAAAACTGCGTGGTGGGAATCCAGGCC
AATACAGAAAGGATCAACAAGCTGATGAATGAGTCTCTAATGTTGGTGACAGCTCTCAAT
CCTCATATAGGGTATGACAAGGCAGCAAAGATTGCTAAGACAGCACACAAAAATGGATCA
ACCTTAAAGGAAACTGCTATCGAACTTGGCTATCTCACAGCAGAGCAGTTTGACGAATGG
GTAAAACCTAAGGACATGCTGGGTCCAAAGTGA

1. Kinsella BT, Doonan S: Nucleotide sequence of a cDNA coding for mitochondrial fumarase from human liver. Biosci Rep. 1986 Oct;6(10):921-9. [PubMed ]
2. Coughlin EM, Christensen E, Kunz PL, Krishnamoorthy KS, Walker V, Dennis NR, Chalmers RA, Elpeleg ON, Whelan D, Pollitt RJ, Ramesh V, Mandell R, Shih VE: Molecular analysis and prenatal diagnosis of human fumarase deficiency. Mol Genet Metab. 1998 Apr;63(4):254-62. [PubMed ]
3. Tomlinson IP, Alam NA, Rowan AJ, Barclay E, Jaeger EE, Kelsell D, Leigh I, Gorman P, Lamlum H, Rahman S, Roylance RR, Olpin S, Bevan S, Barker K, Hearle N, Houlston RS, Kiuru M, Lehtonen R, Karhu A, Vilkki S, Laiho P, Eklund C, Vierimaa O, Aittomaki K, Hietala M, Sistonen P, Paetau A, Salovaara R, Herva R, Launonen V, Aaltonen LA: Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer. Nat Genet. 2002 Apr;30(4):406-10. Epub 2002 Feb 25. [PubMed ]

MYRALRLLARSRPLVRAPAAALASAPGLGGAAVPSFWPPNAARMASQNSFRIEYDTFGEL
KVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYGLDPKIANAI
MKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDH
VNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAV
PLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL
TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPE
NEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSA
RLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGS
TLKETAIELGYLTAEQFDEWVKPKDMLGPK

• Lyase_1 (PF00206 )

• None

• None

MAALLLRHVGRHCLRAHFSPQLCIRNAVPLGTTAKEEMERFWNKNIGSNRPLSPHITIYS
WSLPMAMSICHRGTGIALSADVGPRKRPEDSPAIPVWSGCPGSYCVVLYGAGSHVKKGGS
QHHLPTHYYIHPSFCLSFLSPAWEKFSLFV

• Sdh_cyt (PF01127 )

• None

• None

ATGGCTGCGCTGTTGCTGAGACACGTTGGTCGTCATTGCCTCCGAGCCCACTTTAGCCCT
CAGCTCTGTATCAGAAATGCTGTTCCTTTGGGAACCACGGCCAAAGAAGAGATGGAGCGG
TTCTGGAATAAGAATATAGGTTCAAACCGTCCTCTGTCTCCCCACATTACTATCTACAGT
TGGTCTCTTCCCATGGCGATGTCCATCTGCCACCGTGGCACTGGTATTGCTTTGAGTGCA
GATGTGGGACCTAGGAAAAGGCCTGAAGATTCCCCAGCTATACCAGTCTGGAGTGGTTGT
CCTGGTTCTTACTGTGTTGTCCTCTATGGGGCTGGCAGCCATGTGAAGAAAGGAGGCTCC
CAGCATCATCTTCCTACACATTATTACATTCACCCATCTTTCTGTTTGTCATTCTTATCT
CCAGCCTGGGAAAAGTTCTCCTTATTTGTTTAG

MAALLLRHVGRHCLRAHFSPQLCIRNWSLPMAMSICHRGTGIALSAGVSLFGMSALLLPG
NFESYLELVKSLCLGPALIHTAKFALVFPLMYHTWNGIRHLMWDLGKGLKIPQLYQSGVV
VLVLTVLSSMGLAAM

• Sdh_cyt (PF01127 )

• None

• None

ATGGCTGCGCTGTTGCTGAGACACGTTGGTCGTCATTGCCTCCGAGCCCACTTTAGCCCT
CAGCTCTGTATCAGAAATTGGTCTCTTCCCATGGCGATGTCCATCTGCCACCGTGGCACT
GGTATTGCTTTGAGTGCAGGGGTCTCTCTTTTTGGCATGTCGGCCCTGTTACTCCCTGGG
AACTTTGAGTCTTATTTGGAACTTGTGAAGTCCCTGTGTCTGGGGCCAGCACTGATCCAC
ACAGCTAAGTTTGCACTCGTCTTCCCTCTCATGTATCATACCTGGAATGGGATCCGACAC
TTGATGTGGGACCTAGGAAAAGGCCTGAAGATTCCCCAGCTATACCAGTCTGGAGTGGTT
GTCCTGGTTCTTACTGTGTTGTCCTCTATGGGGCTGGCAGCCATGTGA

1. Wohllk N, Thomas PM, Huang E, Cote GJ: A human succinate-ubiquinone oxidoreductase CII-3 subunit gene ending in a polymorphic dinucleotide repeat is located within the sulfonylurea receptor (SUR) gene. Mol Genet Metab. 1998 Nov;65(3):187-90. [PubMed ]

MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQD
VFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPAT
IGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQM
KPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQ
KWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLS
VNLKGEGMSQAATICKSNFKYMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGPEPENFG
SMLELSWKGTKPIDLGNGQTRKFLLDGDEVIITGYCQGDGYRIGFGQCAGKVLPALLPS

• DUF1969 (PF09298 )
• FAA_hydrolase (PF01557 )

• None

• None

MAAVVALSLRRRLPATTLGGACLQASRGAQTAAATAPRIKKFAIYRWDPDKAGDKPHMQT
YEVDLNKCGPMVLDALIKIKNEVDSTLTFRRSCREGICGSCAMNINGGNTLACTRRIDTN
LNKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPYLKKKDESQEGKQQYLQSIEEREKL
DGLYECILCACCSTSCPSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQDPFSL
YRCHTIMNCTRTCPKGLNPGKAIAEIKKMMATYKEKKASV

• None

• None