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InterPro: IPR016105 Pyruvoyl-dependent histidine/arginine decarboxylase, 3-layer sandwich domain

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UniProtKB

Matches:

161 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

IPR016105 Pyr-dep_his/arg-deCO2ase_sand

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.50.20.10	Pyr-dep_his/arg-deCO2ase_sand	161
Signatures in BioMart

InterPro Relationships Help

Found in

IPR002724 Pyruvoyl-dependent arginine decarboxylase
IPR003427 Pyruvoyl-dependent histidine decarboxylase, PI chain
IPR016004 Pyruvoyl-dependent histidine decarboxylase, PI chain, Gram-positive
IPR016104 Pyruvoyl-dependent histidine/arginine decarboxylase

GO Term annotation Help

Process

GO:0006520 cellular amino acid metabolic process

Function

GO:0016831 carboxy-lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a structural subdomain found in pyruvoyl-dependent histidine decarboxylase (EC:4.1.1.2) and arginine decarboxylase (EC:4.1.1.19). This subdomain consists of a 3-layer beta-beta-alpha sandwich. These proteins form heterohexamers [1, 2].

Histidine decarboxylase catalyses the formation of histamine from histidine. It requires a pyruvoyl group for its activity. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer (alpha beta) 6 by nonhydrolytic self-catalysis.

Arginine decarboxylase catalyses the interconversion of arginine and agmatine plus carbon dioxide. It requires a pyruvoyl group for its activity.

Structural links Help

PDB - click here

SCOP: d.155.1.1 , d.155.1.2

CATH: 3.30.60.30 , 3.50.20.10

Database links Help

Enzyme: EC:4.1.1.19

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR016105

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00862 Histidine decarboxylase proenzyme

Q57764 Pyruvoyl-dependent arginine decarboxylase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002724	Pyruvoyl-dependent arginine decarboxylase
IPR016105	Pyruvoyl-dependent histidine/arginine decarboxylase, 3-layer sandwich domain
IPR003427	Pyruvoyl-dependent histidine decarboxylase, PI chain
IPR016106	Pyruvoyl-dependent histidine decarboxylase, subdomain
IPR016004	Pyruvoyl-dependent histidine decarboxylase, PI chain, Gram-positive
IPR016104	Pyruvoyl-dependent histidine/arginine decarboxylase
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Schelp E, Worley S, Monzingo AF, Ernst S, Robertus JD. pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a. J. Mol. Biol. 306 727-32 2001 [PubMed: 11243783] http://dx.doi.org/10.1006/jmbi.2000.4430
2.	Tolbert WD, Graham DE, White RH, Ealick SE. Pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii: crystal structures of the self-cleaved and S53A proenzyme forms. Structure 11 285-94 2003 [PubMed: 12623016] http://dx.doi.org/10.1016/S0969-2126(03)00026-1

Additional Reading Open in usermanual
	Worley S, Schelp E, Monzingo AF, Ernst S, Robertus JD. Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a. Proteins 46 2002 321-9 [PubMed: 11835507] http://dx.doi.org/10.1002/prot.10042
	Gallagher T, Rozwarski DA, Ernst SR, Hackert ML. Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a. J. Mol. Biol. 230 1993 516-28 [PubMed: 8464063] http://dx.doi.org/10.1006/jmbi.1993.1168
	Soriano EV, McCloskey DE, Kinsland C, Pegg AE, Ealick SE. Structures of the N47A and E109Q mutant proteins of pyruvoyl-dependent arginine decarboxylase from Methanococcus jannaschii. Acta Crystallogr. D Biol. Crystallogr. 64 2008 377-82 [PubMed: 18391404] http://dx.doi.org/10.1107/S0907444908000474

InterPro 23.1