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InterPro: IPR006361 Uroporphyrinogen decarboxylase HemE

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UniProtKB

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1411 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR006361 Uroporphyrinogen_deCO2ase_HemE

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00218	Uroporphyrinogen_deCO2ase_HemE	1099
PANTHER	PTHR21091:SF2	HemE	1400
TIGRFAMs	TIGR01464	hemE	1332
Signatures in BioMart

InterPro Relationships Help

Contains

IPR000257 Uroporphyrinogen decarboxylase (URO-D)

GO Term annotation Help

Process

GO:0006779 porphyrin biosynthetic process

Function

GO:0004853 uroporphyrinogen decarboxylase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents uroporphyrinogen decarboxylase (HemE), which catalyzes the fifth step in the haem biosynthetic pathway, converting uroporphyrinogen III to coproporphyrinogen III by decarboxylating the four acetate side chains of the substrate [1]. This step takes the pathway toward protoporphyrin IX, a common precursor of both haem and chlorophyll, rather than toward precorrin 2 and its products.

This activity is essential in all organisms, and subnormal activity of URO-D leads to the most common form of porphyria in humans, porphyria cutanea tarda (PCT).

Structural links Help

PDB - click here

SCOP: c.1.22.1

CATH: 3.20.20.210

Database links Help

Enzyme: EC:4.1.1.37

CluSTr: ALLvsALL:602:49.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006361

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O22886 Uroporphyrinogen decarboxylase 2, chloroplastic

P06132 Uroporphyrinogen decarboxylase

P32347 Uroporphyrinogen decarboxylase

P70697 Uroporphyrinogen decarboxylase

Q9V595 Uroporphyrinogen decarboxylase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000257	Uroporphyrinogen decarboxylase (URO-D)
IPR006361	Uroporphyrinogen decarboxylase HemE
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Whitby FG, Phillips JD, Kushner JP, Hill CP. Crystal structure of human uroporphyrinogen decarboxylase. EMBO J. 17 2463-71 1998 [PubMed: 9564029] http://dx.doi.org/10.1093/emboj/17.9.2463

Additional Reading Open in usermanual
	Phillips JD, Whitby FG, Stadtmueller BM, Edwards CQ, Hill CP, Kushner JP. Two novel uroporphyrinogen decarboxylase (URO-D) mutations causing hepatoerythropoietic porphyria (HEP). Transl Res 149 2007 85-91 [PubMed: 17240319] http://dx.doi.org/10.1016/j.trsl.2006.08.006
	Phillips JD, Parker TL, Schubert HL, Whitby FG, Hill CP, Kushner JP. Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase. Blood 98 2001 3179-85 [PubMed: 11719352] http://dx.doi.org/10.1182/blood.V98.12.3179
	Phillips JD, Whitby FG, Kushner JP, Hill CP. Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase. EMBO J. 22 2003 6225-33 [PubMed: 14633982] http://dx.doi.org/10.1093/emboj/cdg606
	Fan J, Liu Q, Hao Q, Teng M, Niu L. Crystal structure of uroporphyrinogen decarboxylase from Bacillus subtilis. J. Bacteriol. 189 2007 3573-80 [PubMed: 17122346] http://dx.doi.org/10.1128/JB.01083-06
	Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A. Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism. J. Biol. Chem. 276 2001 44108-16 [PubMed: 11524417] http://dx.doi.org/10.1074/jbc.M104759200

InterPro 23.1