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InterPro: IPR000183 Orn/DAP/Arg decarboxylase 2

Protein matches Help

UniProtKB

Matches:

4879 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR000183 De-COase2

Secondary

IPR002432

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00278	Orn_DAP_Arg_deC	3636
Pfam	PF02784	Orn_Arg_deC_N	4474
PRINTS	PR01179	ODADCRBXLASE	3303
PROSITE pattern	PS00878	ODR_DC_2_1	1928
PROSITE pattern	PS00879	ODR_DC_2_2	1892
Signatures in BioMart

InterPro Relationships Help

Children

IPR002986 Diaminopimelate decarboxylase

Found in

IPR002433 Ornithine decarboxylase
IPR002985 Arginine decarboxylase
IPR005730 Carboxynorspermidine decarboxylase
IPR017530 Pyridoxal-dependent decarboxylase, exosortase system type 1 associated

Contains

IPR009006 Alanine racemase/group IV decarboxylase, C-terminal

GO Term annotation Help

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

These enzymes are collectively known as group IV decarboxylases [1]. Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates can be classified into two different families on the basis of sequence similarities [2, 1]. Members of this family while most probably evolutionary related, do not share extensive regions of sequence similarities. The proteins contain a conserved lysine residue which is known, in mouse ODC [3], to be the site of attachment of the pyridoxal-phosphate group. The proteins also contain a stretch of three consecutive glycine residues and has been proposed to be part of a substrate- binding region [4].

Structural links Help

PDB - click here

SCOP: b.49.2.3 , c.1.6.1

CATH: 2.40.37.10 , 3.20.20.10

Database links Help

PDBe-motif: PS00878 , PS00879

Enzyme: EC:4.1.1

PROSITE doc: PDOC00685

PANDIT: PF00278 , PF02784

Blocks: IPB000183

COMe: PRX000831

Pfam Clan: CL0152.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000183

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35484 Antizyme inhibitor 1

P08432 Ornithine decarboxylase

P11926 Ornithine decarboxylase

P40807 Ornithine decarboxylase 1

P41931 Ornithine decarboxylase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR009006	Alanine racemase/group IV decarboxylase, C-terminal
IPR000183	Orn/DAP/Arg decarboxylase 2
IPR002433	Ornithine decarboxylase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Sandmeier E, Hale TI, Christen P. Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases. Eur. J. Biochem. 221 997-1002 1994 [PubMed: 8181483] http://dx.doi.org/10.1111/j.1432-1033.1994.tb18816.x
2.	Martin C, Cami B, Yeh P, Stragier P, Parsot C, Patte JC. Pseudomonas aeruginosa diaminopimelate decarboxylase: evolutionary relationship with other amino acid decarboxylases. Mol. Biol. Evol. 5 549-59 1988 [PubMed: 3143046] http://mbe.oxfordjournals.org/cgi/content/abstract/5/5/549.pdf
3.	Poulin R, Lu L, Ackermann B, Bey P, Pegg AE. Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites. J. Biol. Chem. 267 150-8 1992 [PubMed: 1730582] http://intl.jbc.org/cgi/reprint/267/1/150.pdf
4.	Moore RC, Boyle SM. Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli. J. Bacteriol. 172 4631-40 1990 [PubMed: 2198270] http://jb.asm.org/cgi/content/abstract/172/8/4631

Additional Reading Open in usermanual
	Kern AD, Oliveira MA, Coffino P, Hackert ML. Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure 7 1999 567-81 [PubMed: 10378276] http://dx.doi.org/10.1016/S0969-2126(99)80073-2
	Dufe VT, Ingner D, Heby O, Khomutov AR, Persson L, Al-Karadaghi S. A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 1-amino-oxy-3-aminopropane. Biochem. J. 405 2007 261-8 [PubMed: 17407445] http://dx.doi.org/10.1042/BJ20070188
	Shah R, Akella R, Goldsmith EJ, Phillips MA. X-ray structure of Paramecium bursaria Chlorella virus arginine decarboxylase: insight into the structural basis for substrate specificity. Biochemistry 46 2007 2831-41 [PubMed: 17305368] http://dx.doi.org/10.1021/bi6023447
	Jackson LK, Baldwin J, Akella R, Goldsmith EJ, Phillips MA. Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase. Biochemistry 43 2004 12990-9 [PubMed: 15476392] http://dx.doi.org/10.1021/bi048933l
	Kefala G, Perry LJ, Weiss MS. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 2005 782-4 [PubMed: 16511157]
	Weyand S, Kefala G, Svergun DI, Weiss MS. The three-dimensional structure of diaminopimelate decarboxylase from Mycobacterium tuberculosis reveals a tetrameric enzyme organisation. J. Struct. Funct. Genomics 10 2009 209-17 [PubMed: 19543810] http://dx.doi.org/10.1007/s10969-009-9065-z

InterPro 23.1