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Human Metabolome Database Version 2.5

 

Showing metabocard for Uroporphyrinogen I (HMDB02211)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:42
Update Date 2009-05-05 20:59:17
Accession Number HMDB02211
Secondary Accession Numbers Not Available
Common Name Uroporphyrinogen I
Description Uroporphyrinogens are porphyrinogen variants in which each pyrrole ring has one acetate side chain and one propionate side chain; it is formed by condensation 4 four molecules of porphobilinogen. 4 isomers are possible but only 2 commoly are found, types I and III. Uroporphyrinogen III is a functional intermediate in heme biosynthesis while Uroporphyrinogen I is produced in an abortive side reaction.
Synonyms
  1. 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro-21H,23H-Porphine-2,7,12,17-tetrapropanoic acid
  2. 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro-(8CI)-2,7,12,17-Porphinetetrapropionate
  3. 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro-(8CI)-2,7,12,17-Porphinetetrapropionic acid
  4. 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydroporphyrin-2,7,12,17-tetrapropanoate
  5. 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydroporphyrin-2,7,12,17-tetrapropanoic acid
  6. 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro-21H,23H-Porphine-2,7,12,17-tetrapropanoate
Chemical IUPAC Name 3,8,13,18-tetrakis(carboxymethyl)-5,10,15,20,22,24-hexahydro 21H,23H-Porphine-2,7,12,17-tetrapropanoic acid
Chemical Formula C40H44N4O16
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Heterocyclic molecules
Class
  • Porphyrins
Sub Class
  • Uroporphyrins
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • aromatic compound
  • heterocyclic compound
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 836.795
Monoisotopic Molecular Weight 836.275208
Isomeric SMILES OC(=O)CCC1=C2CC3=C(CC(O)=O)C(CCC(O)=O)=C(CC4=C(CC(O)=O)C(CCC(O)=O)=C(CC5=C(CC(O)=O)C(CCC(O)=O)=C(CC(N2)=C1CC(O)=O)N5)N4)N3
Canonical SMILES OC(=O)CCC1=C2CC3=C(CC(O)=O)C(CCC(O)=O)=C(CC4=C(CC(O)=O)C(CCC(O)=O)=C(CC5=C(CC(O)=O)C(CCC(O)=O)=C(CC(N2)=C1CC(O)=O)N5)N4)N3
KEGG Compound ID C05766 Link Image
BioCyc ID UROPORPHYRINOGEN-III Link Image
BiGG ID Not Available
Wikipedia Link Uroporphyrinogen I Link Image
NuGOwiki Link HMDB02211 Link Image
Metagene Link HMDB02211 Link Image
METLIN ID 6550 Link Image
PubChem Compound 440775 Link Image
PubChem Substance 8061 Link Image
ChEBI ID 28766 Link Image
CAS Registry Number 1867-62-5
InChI Identifier InChI=1/C40H44N4O16/c45-33(46)5-1-17-21(9-37(53)54)29-14-26-19(3-7-35(49)50)23(11-39(57)58)31(43-26)16-28-20(4-8-36(51)52)24(12-40(59)60)32(44-28)15-27-18(2-6-34(47)48)22(10-38(55)56)30(42-27)13-25(17)41-29/h41-44H,1-16H2,(H,45,46)(H,47,48)(H,49,50)(H,51,52)(H,53,54)(H,55,56)(H,57,58)(H,59,60)
Synthesis Reference Burton, Gerardo; Fagerness, Paul E.; Hosozawa, Shigeki; Jordan, Peter M.; Scott, A. Ian. Carbon-13 NMR evidence for a new intermediate, pre-uroporphyrinogen, in the enzymic transformation of porphobilinogen into uroporphyrinogens I and III. Journal of the Chemical Society, Chemical Communications (1979), (5), 202-4.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.0437 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -8
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.67 [Predicted by ALOGPS]; -2.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location Not Available
Biofluid Location Not Available
Tissue Location
Tissue References
Testes —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Porphyrin Metabolism SMP00024 Link Image map00860 Link Image
General References
  1. Maines MD, Mayer RD: Inhibition of testicular cytochrome P-450-dependent steroid biosynthesis by cis-platinum. Reversal by human chorionic gonadotropin. J Biol Chem. 1985 May 25;260(10):6063-8. [PubMed Link Image]
  2. Mukerji SK, Pimstone NR: Defective human erythrocyte uroporphyrinogen decarboxylase in familial porphyria cutanea tarda: the metabolic lesion or the result of endogenous porphyrinemia? Biochem Biophys Res Commun. 1988 Jul 15;154(1):39-46. [PubMed Link Image]
  3. Wikipedia Link Image
Metabolic Enzymes
  1. Uroporphyrinogen decarboxylase
  2. Uroporphyrinogen-III synthase
  3. cDNA FLJ76900, highly similar to Homo sapiens uroporphyrinogen decarboxylase
  4. Uroporphyrinogen decarboxylase (EC 4.1.1.37)
  5. Uroporphyrinogen decarboxylase (EC 4.1.1.37)
Enzyme 1 [top]
Enzyme 1 ID 5482
Enzyme 1 Name Uroporphyrinogen decarboxylase
Enzyme 1 Synonyms
  1. URO-D
  2. UPD
Enzyme 1 Gene Name UROD
Enzyme 1 Protein Sequence >Uroporphyrinogen decarboxylase 
MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCR
SPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLER
LRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRW
LYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDV
AKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVT
LQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKH
SRLLRQN
Enzyme 1 Number of Residues 367
Enzyme 1 Molecular Weight 40787
Enzyme 1 Theoretical pI 6.06
Enzyme 1 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
  • uroporphyrinogen decarboxylase activity
Process
  • cellular metabolism
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 1 General Function Coenzyme transport and metabolism
Enzyme 1 Specific Function Uroporphyrinogen III = coproporphyrinogen + 4 CO(2)
Enzyme 1 Pathways
Enzyme 1 Reactions
  • uroporphyrinogen III = coproporphyrinogen + 4 CO2
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 340181 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P06132 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DCUP_HUMAN Link Image
Enzyme 1 PDB ID 1R3Y Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1104 bp 
ATGGAAGCGAATGGGTTGGGACCTCAGGGTTTTCCGGAGCTGAAGAATGACACATTCCTG
CGAGCAGCTTGGGGAGAGGAAACAGACTACACTCCCGTTTGGTGCATGCGCCAGGCAGGC
CGTTACTTACCAGAGTTTAGGGAAACCCGGGCTGCCCAGGACTTTTTCAGCACGTGTCGC
TCTCCTGAGGCCTGCTGTGAACTGACTCTGCAGCCACTGCGTCGCTTCCCTCTGGATGCT
GCCATCATTTTCTCCGACATCCTTGTTGTACCCCAGGCACTGGGCATGGAGGTGACCATG
GTACCTAGCAAAGGACCCAGCTTCCCAGAGCCATTAAGAGAAGAGCAGGACCTAGAAGCG
CTACGGGATCCAGAAGTGGTAGCCTCTGAGCTAGGCTATGTGTTCCAAGCCATCACCCTT
ACCCGACAACGACTGGCTGGACGTGTGCCGCTGATTGGCTTTGCTGGTGCCCCATGGACC
CTGATGACATACATGGTTGAGGGTGGTGGCTCAAGCACCATGGCTCAGGCCAAGCGCTGG
CTCTATCAGAGACCTCAGGCTAGTCACCAGCTGCTTCGCATCCTCACTGATGCTCTGGTC
CCATATCTGGTAGGACAAGTGGTGGCTGGTGCCCAGGCATTGCAGCTGTTTGAGTCCCAT
GCAGGGCATCTTGGCCCACAGCTCTTCAACAAGTTTGCACTGCCTTACATCCGTGATGTG
GCCAAGCAAGTGAAGGCCAGGTTGCGGGAGGCAGGCCTGGCACCAGTGCCCATGATCATC
TTTGCTAAGGATGGGCATTTTGCCCTGGAGGAGCTGGCCCAAGCTGGCTATGAGGTGGTT
GGGCTTGACTGGACAGTGGCCCCAAAGAAAGCCCGGGAGTGTGTGGGGAAGACGGTGACA
TTGCAGGGCAACTTGGACCCCTGTGCCTTGTATGCATCTGAGGAGGAGATCGGGCAGTTG
GTGAAGCAGATGCTGGATGACTTTGGACCACATCGCTACATTGCCAACTTGGGCCATGGG
CTTTATCCTGACATGGACCCAGAACATGTGGGCGCCTTTGTGGATGCTGTGCATAAACAC
TCACGTCTGCTTCGACAGAACTGA
Enzyme 1 GenBank Gene ID M14016 Link Image
Enzyme 1 GeneCard ID UROD Link Image
Enzyme 1 GenAtlas ID UROD Link Image
Enzyme 1 HGNC ID HGNC:12591 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p34
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Romeo PH, Raich N, Dubart A, Beaupain D, Pryor M, Kushner J, Cohen-Solal M, Goossens M: Molecular cloning and nucleotide sequence of a complete human uroporphyrinogen decarboxylase cDNA. J Biol Chem. 1986 Jul 25;261(21):9825-31. [PubMed Link Image]
  2. Moran-Jimenez MJ, Ged C, Romana M, Enriquez De Salamanca R, Taieb A, Topi G, D'Alessandro L, de Verneuil H: Uroporphyrinogen decarboxylase: complete human gene sequence and molecular study of three families with hepatoerythropoietic porphyria. Am J Hum Genet. 1996 Apr;58(4):712-21. [PubMed Link Image]
  3. Romana M, Dubart A, Beaupain D, Chabret C, Goossens M, Romeo PH: Structure of the gene for human uroporphyrinogen decarboxylase. Nucleic Acids Res. 1987 Sep 25;15(18):7343-56. [PubMed Link Image]
  4. Garey JR, Harrison LM, Franklin KF, Metcalf KM, Radisky ES, Kushner JP: Uroporphyrinogen decarboxylase: a splice site mutation causes the deletion of exon 6 in multiple families with porphyria cutanea tarda. J Clin Invest. 1990 Nov;86(5):1416-22. [PubMed Link Image]
  5. Whitby FG, Phillips JD, Kushner JP, Hill CP: Crystal structure of human uroporphyrinogen decarboxylase. EMBO J. 1998 May 1;17(9):2463-71. [PubMed Link Image]
  6. Phillips JD, Parker TL, Schubert HL, Whitby FG, Hill CP, Kushner JP: Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase. Blood. 2001 Dec 1;98(12):3179-85. [PubMed Link Image]
  7. de Verneuil H, Grandchamp B, Beaumont C, Picat C, Nordmann Y: Uroporphyrinogen decarboxylase structural mutant (Gly281----Glu) in a case of porphyria. Science. 1986 Nov 7;234(4777):732-4. [PubMed Link Image]
  8. Garey JR, Hansen JL, Harrison LM, Kennedy JB, Kushner JP: A point mutation in the coding region of uroporphyrinogen decarboxylase associated with familial porphyria cutanea tarda. Blood. 1989 Mar;73(4):892-5. [PubMed Link Image]
  9. Romana M, Grandchamp B, Dubart A, Amselem S, Chabret C, Nordmann Y, Goossens M, Romeo PH: Identification of a new mutation responsible for hepatoerythropoietic porphyria. Eur J Clin Invest. 1991 Apr;21(2):225-9. [PubMed Link Image]
  10. de Verneuil H, Bourgeois F, de Rooij F, Siersema PD, Wilson JH, Grandchamp B, Nordmann Y: Characterization of a new mutation (R292G) and a deletion at the human uroporphyrinogen decarboxylase locus in two patients with hepatoerythropoietic porphyria. Hum Genet. 1992 Jul;89(5):548-52. [PubMed Link Image]
  11. Meguro K, Fujita H, Ishida N, Akagi R, Kurihara T, Galbraith RA, Kappas A, Zabriskie JB, Toback AC, Harber LC, et al.: Molecular defects of uroporphyrinogen decarboxylase in a patient with mild hepatoerythropoietic porphyria. J Invest Dermatol. 1994 May;102(5):681-5. [PubMed Link Image]
  12. Roberts AG, Elder GH, De Salamanca RE, Herrero C, Lecha M, Mascaro JM: A mutation (G281E) of the human uroporphyrinogen decarboxylase gene causes both hepatoerythropoietic porphyria and overt familial porphyria cutanea tarda: biochemical and genetic studies on Spanish patients. J Invest Dermatol. 1995 Apr;104(4):500-2. [PubMed Link Image]
  13. McManus JF, Begley CG, Sassa S, Ratnaike S: Five new mutations in the uroporphyrinogen decarboxylase gene identified in families with cutaneous porphyria. Blood. 1996 Nov 1;88(9):3589-600. [PubMed Link Image]
  14. Mendez M, Sorkin L, Rossetti MV, Astrin KH, del C Batlle AM, Parera VE, Aizencang G, Desnick RJ: Familial porphyria cutanea tarda: characterization of seven novel uroporphyrinogen decarboxylase mutations and frequency of common hemochromatosis alleles. Am J Hum Genet. 1998 Nov;63(5):1363-75. [PubMed Link Image]
  15. McManus JF, Begley CG, Sassa S, Ratnaike S: Three new mutations in the uroporphyrinogen decarboxylase gene in familial porphyria cutanea tarda. Mutation in brief no. 237. Online. Hum Mutat. 1999;13(5):412. [PubMed Link Image]
  16. Christiansen L, Ged C, Hombrados I, Brons-Poulsen J, Fontanellas A, de Verneuil H, Horder M, Petersen NE: Screening for mutations in the uroporphyrinogen decarboxylase gene using denaturing gradient gel electrophoresis. Identification and characterization of six novel mutations associated with familial PCT. Hum Mutat. 1999;14(3):222-32. [PubMed Link Image]
  17. Brady JJ, Jackson HA, Roberts AG, Morgan RR, Whatley SD, Rowlands GL, Darby C, Shudell E, Watson R, Paiker J, Worwood MW, Elder GH: Co-inheritance of mutations in the uroporphyrinogen decarboxylase and hemochromatosis genes accelerates the onset of porphyria cutanea tarda. J Invest Dermatol. 2000 Nov;115(5):868-74. [PubMed Link Image]
  18. Cappellini MD, Martinez di Montemuros F, Tavazzi D, Fargion S, Pizzuti A, Comino A, Cainelli T, Fiorelli G: Seven novel point mutations in the uroporphyrinogen decarboxylase (UROD) gene in patients with familial porphyria cutanea tarda (f-PCT). Hum Mutat. 2001 Apr;17(4):350. [PubMed Link Image]
  19. Ged C, Ozalla D, Herrero C, Lecha M, Mendez M, de Verneuil H, Mascaro JM: Description of a new mutation in hepatoerythropoietic porphyria and prenatal exclusion of a homozygous fetus. Arch Dermatol. 2002 Jul;138(7):957-60. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5593
Enzyme 2 Name Uroporphyrinogen-III synthase
Enzyme 2 Synonyms
  1. UROS
  2. Uroporphyrinogen- III cosynthetase
  3. Hydroxymethylbilane hydrolyase [cyclizing]
  4. UROIIIS
Enzyme 2 Gene Name UROS
Enzyme 2 Protein Sequence >Uroporphyrinogen-III synthase 
MKVLLLKDAKEDDCGQDPYIRELGLYGLEATLIPVLSFEFLSLPSFSEKLSHPEDYGGLI
FTSPRAVEAAELCLEQNNKTEVWERSLKEKWNAKSVYVVGNATASLVSKIGLDTEGETCG
NAEKLAEYICSRESSALPLLFPCGNLKREILPKALKDKGIAMESITVYQTVAHPGIQGNL
NSYYSQQGVPASITFFSPSGLTYSLKHIQELSGDNIDQIKFAAIGPTTARALAAQGLPVS
CTAESPTPQALATGIRKALQPHGCC
Enzyme 2 Number of Residues 265
Enzyme 2 Molecular Weight 28628
Enzyme 2 Theoretical pI 5.16
Enzyme 2 GO Classification
Function
  • carbon-oxygen lyase activity
  • catalytic activity
  • hydro-lyase activity
  • lyase activity
  • uroporphyrinogen-III synthase activity
Process
  • cellular metabolism
  • heme biosynthesis
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 2 General Function Coenzyme transport and metabolism
Enzyme 2 Specific Function Hydroxymethylbilane = uroporphyrinogen III + H(2)O
Enzyme 2 Pathways
Enzyme 2 Reactions
  • hydroxymethylbilane = uroporphyrinogen III + H2O
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 337463 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P10746 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name HEM4_HUMAN Link Image
Enzyme 2 PDB ID 1JR2 Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >798 bp 
ATGAAGGTTCTTTTACTGAAGGATGCGAAGGAAGATGACTGTGGCCAGGATCCGTATATC
AGGGAATTAGGATTATATGGACTTGAAGCCACTTTGATCCCTGTTTTATCGTTTGAGTTT
TTGTCTCTTCCCAGTTTCTCTGAGAAGCTTTCTCATCCTGAAGATTACGGGGGACTCATT
TTTACCAGCCCCAGAGCAGTGGAAGCAGCAGAGTTATGTTTGGAGCAAAACAATAAAACT
GAAGTCTGGGAAAGGTCTCTGAAAGAAAAATGGAATGCCAAGTCAGTGTATGTGGTTGGA
AATGCTACTGCTTCTCTAGTGAGTAAAATTGGCCTGGATACAGAAGGAGAAACCTGTGGA
AATGCAGAAAAGCTTGCAGAATATATTTGTTCCAGGGAGTCCTCAGCACTGCCTCTTCTA
TTTCCCTGTGGAAACCTCAAAAGAGAAATCCTGCCAAAAGCGCTCAAGGACAAAGGGATT
GCCATGGAAAGCATAACTGTGTATCAGACAGTTGCACACCCAGGAATCCAAGGGAACCTG
AACAGCTACTATTCCCAGCAGGGGGTTCCAGCCAGCATCACATTTTTTAGTCCCTCTGGC
CTCACATACAGTCTCAAGCACATTCAGGAGTTATCTGGTGACAATATCGATCAAATTAAG
TTTGCAGCCATCGGCCCCACTACGGCTCGCGCGCTGGCCGCCCAGGGCCTTCCTGTAAGC
TGCACTGCAGAGAGCCCCACGCCACAAGCCCTGGCCACTGGCATCAGGAAGGCTCTCCAG
CCCCATGGCTGCTGCTGA
Enzyme 2 GenBank Gene ID J03824 Link Image
Enzyme 2 GeneCard ID UROS Link Image
Enzyme 2 GenAtlas ID UROS Link Image
Enzyme 2 HGNC ID HGNC:12592 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q25.2-q26.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Tsai SF, Bishop DF, Desnick RJ: Human uroporphyrinogen III synthase: molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7049-53. [PubMed Link Image]
  2. Xu W, Astrin KH, Desnick RJ: Molecular basis of congenital erythropoietic porphyria: mutations in the human uroporphyrinogen III synthase gene. Hum Mutat. 1996;7(3):187-92. [PubMed Link Image]
  3. Deybach JC, de Verneuil H, Boulechfar S, Grandchamp B, Nordmann Y: Point mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria (Gunther's disease). Blood. 1990 May 1;75(9):1763-5. [PubMed Link Image]
  4. Boulechfar S, Da Silva V, Deybach JC, Nordmann Y, Grandchamp B, de Verneuil H: Heterogeneity of mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria. Hum Genet. 1992 Jan;88(3):320-4. [PubMed Link Image]
  5. Warner CA, Yoo HW, Roberts AG, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of exonic mutations in the uroporphyrinogen III synthase gene. J Clin Invest. 1992 Feb;89(2):693-700. [PubMed Link Image]
  6. Xu W, Warner CA, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of 10 mutations in the uroporphyrinogen III synthase gene. J Clin Invest. 1995 Feb;95(2):905-12. [PubMed Link Image]
  7. Tanigawa K, Bensidhoum M, Takamura N, Namba H, Yamashita S, de Verneuil H, Ged C: A novel point mutation in congenital erythropoietic porphyria in two members of Japanese family. Hum Genet. 1996 May;97(5):557-60. [PubMed Link Image]
  8. Tezcan I, Xu W, Gurgey A, Tuncer M, Cetin M, Oner C, Yetgin S, Ersoy F, Aizencang G, Astrin KH, Desnick RJ: Congenital erythropoietic porphyria successfully treated by allogeneic bone marrow transplantation. Blood. 1998 Dec 1;92(11):4053-8. [PubMed Link Image]
  9. Frank J, Wang X, Lam HM, Aita VM, Jugert FK, Goerz G, Merk HF, Poh-Fitzpatrick MB, Christiano AM: C73R is a hotspot mutation in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria. Ann Hum Genet. 1998 May;62(Pt 3):225-30. [PubMed Link Image]
  10. Rogounovitch T, Takamura N, Hombrados I, Morel C, Tanaka T, Kameyoshi Y, Shimizu-Yoshida Y, de Verneuil H, Yamashita S: Congenital erythropoietic porphyria: a novel homozygous mutation in a Japanese patient. J Invest Dermatol. 2000 Dec;115(6):1156. [PubMed Link Image]
  11. Shady AA, Colby BR, Cunha LF, Astrin KH, Bishop DF, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of eight novel mutations in the uroporphyrinogen III synthase gene. Br J Haematol. 2002 Jun;117(4):980-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13084
Enzyme 3 Name cDNA FLJ76900, highly similar to Homo sapiens uroporphyrinogen decarboxylase
Enzyme 3 Synonyms
  1. UROD, mRNA
  2. Uroporphyrinogen decarboxylase, isoform CRA_a
Enzyme 3 Gene Name UROD
Enzyme 3 Protein Sequence >cDNA FLJ76900, highly similar to Homo sapiens uroporphyrinogen decarboxylase 
MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCR
SPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLER
LRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRW
LYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDV
AKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVT
LQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKH
SRLLRQN
Enzyme 3 Number of Residues 367
Enzyme 3 Molecular Weight 40787
Enzyme 3 Theoretical pI 6.06
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Coenzyme transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function Not Available
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 158257186 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A8K762 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A8K762_HUMAN Link Image
Enzyme 3 PDB ID 1R3Y Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AK291877 Link Image
Enzyme 3 GeneCard ID A8K762 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 14934
Enzyme 4 Name Uroporphyrinogen decarboxylase (EC 4.1.1.37)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name Not Available
Enzyme 4 Protein Sequence >Uroporphyrinogen decarboxylase (EC 4.1.1.37) 
MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCR
SPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLER
LRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRW
LYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDV
AKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVT
LQVNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKH
SRLLRQN
Enzyme 4 Number of Residues 367
Enzyme 4 Molecular Weight 40829
Enzyme 4 Theoretical pI 6.06
Enzyme 4 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
  • uroporphyrinogen decarboxylase activity
Process
  • cellular metabolism
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 4 General Function Coenzyme transport and metabolism
Enzyme 4 Specific Function Uroporphyrinogen III = coproporphyrinogen + 4 CO(2)
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • uroporphyrinogen III = coproporphyrinogen III + 4 CO2 [RN:R03197] ALL_REAC R03197
  • (other) R04972
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 30582313 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q53YB8 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q53YB8_HUMAN Link Image
Enzyme 4 PDB ID 1R3Y Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1104 bp 
ATGGAAGCGAATGGGTTGGGACCTCAGGGTTTTCCGGAGCTGAAGAATGACACATTCCTG
CGAGCAGCCTGGGGAGAGGAAACAGACTACACTCCCGTTTGGTGCATGCGCCAGGCAGGC
CGTTACTTACCAGAGTTTAGGGAAACCCGGGCTGCCCAGGACTTTTTCAGCACGTGTCGC
TCTCCTGAGGCCTGCTGTGAACTGACTCTGCAGCCACTGCGTCGCTTCCCTCTGGATGCT
GCCATCATTTTCTCCGACATCCTTGTTGTACCCCAGGCACTGGGCATGGAGGTGACCATG
GTACCTGGCAAAGGACCCAGCTTCCCAGAGCCATTAAGAGAAGAGCAGGACCTAGAACGC
CTACGGGATCCAGAAGTGGTAGCCTCTGAGCTAGGCTATGTGTTCCAAGCCATCACCCTT
ACCCGACAACGACTGGCTGGACGTGTGCCGCTGATTGGCTTTGCTGGTGCCCCATGGACC
CTGATGACATACATGGTTGAGGGTGGTGGCTCAAGCACCATGGCTCAGGCCAAGCGCTGG
CTCTATCAGAGACCTCAGGCTAGTCACCAGCTGCTTCGCATCCTCACTGATGCTCTGGTC
CCATATCTGGTAGGACAAGTGGTGGCTGGTGCCCAGGCATTGCAGCTGTTTGAGTCCCAT
GCAGGGCATCTTGGCCCACAGCTCTTCAACAAGTTTGCACTGCCTTACATCCGTGATGTG
GCCAAGCAAGTGAAGGCCAGGTTGCGGGAGGCAGGCCTGGCACCAGTGCCCATGATCATC
TTTGCTAAGGATGGGCATTTTGCCCTGGAGGAGCTGGCCCAAGCTGGCTATGAGGTGGTT
GGGCTTGACTGGACAGTGGCCCCAAAGAAAGCCCGGGAGTGTGTGGGGAAGACGGTGACA
TTGCAGGTCAACCTGGACCCCTGTGCCTTGTATGCATCTGAGGAGGAGATCGGGCAGTTG
GTGAAGCAGATGCTGGATGACTTTGGACCACATCGCTACATTGCCAACCTGGGCCATGGG
CTTTATCCTGACATGGACCCAGAACATGTGGGCGCCTTTGTGGATGCTGTGCATAAACAC
TCACGTCTGCTTCGACAGAACTAG
Enzyme 4 GenBank Gene ID BT006737 Link Image
Enzyme 4 GeneCard ID Q53YB8 Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID HGNC:12591 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs Not Available
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 14935
Enzyme 5 Name Uroporphyrinogen decarboxylase (EC 4.1.1.37)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name UROD
Enzyme 5 Protein Sequence >Uroporphyrinogen decarboxylase (EC 4.1.1.37) 
MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCR
SPEACCELTLQPLRRFLLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLER
LRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRW
LYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDV
AKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVT
LQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKH
SRLLRQN
Enzyme 5 Number of Residues 367
Enzyme 5 Molecular Weight 40803
Enzyme 5 Theoretical pI 6.06
Enzyme 5 GO Classification
Function
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • lyase activity
  • uroporphyrinogen decarboxylase activity
Process
  • cellular metabolism
  • heterocycle metabolism
  • metabolism
  • physiological process
  • porphyrin biosynthesis
  • porphyrin metabolism
Component
—
Enzyme 5 General Function Coenzyme transport and metabolism
Enzyme 5 Specific Function Uroporphyrinogen III = coproporphyrinogen + 4 CO(2)
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • uroporphyrinogen III = coproporphyrinogen III + 4 CO2 [RN:R03197] ALL_REAC R03197
  • (other) R04972
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 31323304 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q53ZP6 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q53ZP6_HUMAN Link Image
Enzyme 5 PDB ID 1R3Y Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1104 bp 
ATGGAAGCGAATGGGTTGGGACCTCAGGGTTTTCCGGAGCTGAAGAATGACACATTCCTG
CGAGCAGCCTGGGGAGAGGAAACAGACTACACTCCCGTTTGGTGCATGCGCCAGGCAGGC
CGTTACTTACCAGAGTTTAGGGAAACCCGGGCTGCCCAGGACTTTTTCAGCACGTGTCGC
TCTCCTGAGGCCTGCTGTGAACTGACTCTGCAGCCACTGCGTCGCTTCCTTCTGGATGCT
GCCATCATTTTCTCCGACATCCTTGTTGTACCCCAGGCACTGGGCATGGAGGTGACCATG
GTACCTGGCAAAGGACCCAGCTTCCCAGAGCCATTAAGAGAAGAGCAGGACCTAGAACGC
CTACGGGATCCAGAAGTGGTAGCCTCTGAGCTAGGCTATGTGTTCCAAGCCATCACCCTT
ACCCGACAACGACTGGCTGGACGTGTGCCGCTGATTGGCTTTGCTGGTGCCCCATGGACC
CTGATGACATACATGGTTGAGGGTGGTGGCTCAAGCACCATGGCTCAGGCCAAGCGCTGG
CTCTATCAGAGACCTCAGGCTAGTCACCAGCTGCTTCGCATCCTCACTGATGCTCTGGTC
CCATATCTGGTAGGACAAGTGGTGGCTGGTGCCCAGGCATTGCAGCTGTTTGAGTCCCAT
GCAGGGCATCTTGGCCCACAGCTCTTCAACAAGTTTGCACTGCCTTACATCCGTGATGTG
GCCAAGCAAGTGAAGGCCAGGTTGCGGGAGGCAGGCCTGGCACCAGTGCCCATGATCATC
TTTGCTAAGGATGGGCATTTTGCCCTGGAGGAGCTGGCCCAAGCTGGCTATGAGGTGGTT
GGGCTTGACTGGACAGTGGCCCCAAAGAAAGCCCGGGAGTGTGTGGGGAAGACGGTGACA
TTGCAGGGCAACCTGGACCCCTGTGCCTTGTATGCATCTGAGGAGGAGATCGGGCAGTTG
GTGAAGCAGATGCTGGATGACTTTGGACCACATCGCTACATTGCCAACCTGGGCCATGGG
CTTTATCCTGACATGGACCCAGAACATGTGGGCGCCTTTGTGGATGCTGTGCATAAACAC
TCACGTCTGCTTCGACAGAACTGA
Enzyme 5 GenBank Gene ID AY292986 Link Image
Enzyme 5 GeneCard ID Q53ZP6 Link Image
Enzyme 5 GenAtlas ID UROD Link Image
Enzyme 5 HGNC ID HGNC:12591 Link Image
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References Not Available
Enzyme 5 Metabolite References Not Available