EzCatDB: S00237

DB codeS00237
CATH domainDomain 13.20.20.210Catalytic domain
E.C.4.1.1.37
CSA1uro


Enzyme Name
Swiss-protKEGG

P06132
Protein nameUroporphyrinogen decarboxylaseuroporphyrinogen decarboxylase
uroporphyrinogen III decarboxylase
porphyrinogen carboxy-lyase
porphyrinogen decarboxylase
uroporphyrinogen-III carboxy-lyase
SynonymsURO-D
UPD
EC 4.1.1.37

KEGG pathways
MAP codePathways
MAP00860Porphyrin and chlorophyll metabolism

Swiss-prot:Accession NumberP06132
Entry nameDCUP_HUMAN
ActivityUroporphyrinogen III = coproporphyrinogen + 4 CO(2).
SubunitHomodimer.
Subcellular locationCytoplasm.
Cofactor


SubstratesProducts
KEGG-idC01051C00011C03263
CompoundUroporphyrinogen IIICO2Coproporphyrinogen III
Typearomatic ring (with nitrogen atoms),carboxyl groupothersaromatic ring (with nitrogen atoms),carboxyl group
1uroAUnboundUnboundUnbound
1jphAUnboundUnboundUnbound
1jpiAUnboundUnboundUnbound
1jpkAUnboundUnboundUnbound

Active-site residues
resource
literature;[8]
pdbCatalytic residuescomment
1uroAASP 86

1jphAASP 86
mutant I260T
1jpiAASP 86
mutant F232L
1jpkAASP 86
mutant G156D

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Scheme 11, p.27-284
[5]Scheme 3, p.134-1373
[8]p.2467-2468

references
[1]
PubMed ID3895052
JournalNat Prod Rep
Year1985
Volume2
Pages19-47
AuthorsLeeper FJ
TitleThe biosynthesis of porphyrins, chlorophylls, and vitamin B12.
[2]
CommentsVARIANT PCT GLU-281.
Medline ID87042763
PubMed ID3775362
JournalScience
Year1986
Volume234
Pages732-4
Authorsde Verneuil H, Grandchamp B, Beaumont C, Picat C, Nordmann Y
TitleUroporphyrinogen decarboxylase structural mutant (Gly281----Glu) in a case of porphyria.
Related Swiss-protP06132
[3]
PubMed ID2180703
JournalEur J Biochem
Year1990
Volume188
Pages393-403
AuthorsFelix F, Brouillet N
TitlePurification and properties of uroporphyrinogen decarboxylase from Saccharomyces cerevisiae. Yeast uroporphyrinogen decarboxylase.
[4]
PubMed ID1576986
JournalEur J Biochem
Year1992
Volume205
Pages1011-6
AuthorsGarey JR, Labbe-Bois R, Chelstowska A, Rytka J, Harrison L, Kushner J, Labbe P
TitleUroporphyrinogen decarboxylase in Saccharomyces cerevisiae. HEM12 gene sequence and evidence for two conserved glycines essential for enzymatic activity.
[5]
PubMed ID7842850
JournalCiba Found Symp
Year1994
Volume180
Pages131-51; discussion 152-5
AuthorsAkhtar M
TitleThe modification of acetate and propionate side chains during the biosynthesis of haem and chlorophylls: mechanistic and stereochemical studies.
[6]
PubMed ID9194196
JournalProtein Sci
Year1997
Volume6
Pages1343-6
AuthorsPhillips JD, Whitby FG, Kushner JP, Hill CP
TitleCharacterization and crystallization of human uroporphyrinogen decarboxylase.
[7]
PubMed ID9761933
JournalActa Crystallogr D Biol Crystallogr
Year1998
Volume54
Pages476-8
AuthorsLaterriere M, d'Estaintot BL, Dautant A, Precigoux G, Hombrados I, De Verneuil H
TitleExpression, purification, crystallization and preliminary X-ray diffraction analysis of human uroporphyrinogen decarboxylase.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID98232492
PubMed ID9564029
JournalEMBO J
Year1998
Volume17
Pages2463-71
AuthorsWhitby FG, Phillips JD, Kushner JP, Hill CP
TitleCrystal structure of human uroporphyrinogen decarboxylase.
Related PDB1uro
Related Swiss-protP06132
[9]
PubMed ID11719352
JournalBlood
Year2001
Volume98
Pages3179-85
AuthorsPhillips JD, Parker TL, Schubert HL, Whitby FG, Hill CP, Kushner JP
TitleFunctional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase.
Related PDB1jph,1jpi,1jpk


createdupdated
2004-03-302009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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