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InterPro: IPR014033 Arginase, subgroup

Protein matches Help

UniProtKB

Matches:

623 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

IPR014033 Arginase_sub

Secondary

IPR005924

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR11358:SF2	Arginase_sub	600
TIGRFAMs	TIGR01229	rocF_arginase	538
Signatures in BioMart

InterPro Relationships Help

Parent

IPR005924 Arginase

Contains

IPR020855 Ureohydrolase, manganese-binding site

GO Term annotation Help

Process

GO:0006525 arginine metabolic process

Function

GO:0004053 arginase activity
GO:0046872 metal ion binding

InterPro annotation

Entry Details in BioMart

Abstract

L-Arginine is converted to nitric oxide and citrulline by the enzyme nitric oxide synthase and by the enzyme arginase as a part of the hepatic urea cycle. Arginase is a manganese metalloenzyme containing a metal-activated hydroxide ion, a critical nucleophile in metalloenzymes that catalyze hydrolysis or hydration reactions. A hydrogen bond formed by the metal-bound hydroxide holds the enzyme in the proper orientation for catalysis however non-metal substrate-binding sites are also implicated in the enzyme mechanism. Regeneration of metal-bound hydroxide ion from a metal-bound water molecule requires proton transfer to bulk solvent mediated by a histidine proton shuttle residue.

Structural links Help

PDB - click here

SCOP: c.42.1.1

CATH: 3.40.800.10

Database links Help

Enzyme: EC:3.5.3.1

PRIAM: PRI000577

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR014033

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O08691 Arginase-2, mitochondrial

P00812 Arginase

P05089 Arginase-1

P07824 Arginase-1

P53608 Arginase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014033	Arginase, subgroup
IPR006035	Ureohydrolase
IPR020855	Ureohydrolase, manganese-binding site
IPR005924	Arginase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW. Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response. Proc. Natl. Acad. Sci. U.S.A. 102 2005 13058-63 [PubMed: 16141327] http://dx.doi.org/10.1073/pnas.0504027102
	Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE. Probing the role of the hyper-reactive histidine residue of arginase. Arch. Biochem. Biophys. 444 2005 15-26 [PubMed: 16266687] http://dx.doi.org/10.1016/j.abb.2005.09.009
	Di Costanzo L, Pique ME, Christianson DW. Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster. J. Am. Chem. Soc. 129 2007 6388-9 [PubMed: 17469833] http://dx.doi.org/10.1021/ja071567j
	Sekowska A, Danchin A, Risler JL. Phylogeny of related functions: the case of polyamine biosynthetic enzymes. Microbiology (Reading, Engl.) 146 ( Pt 8) 2000 1815-28 [PubMed: 10931887]
	Di Costanzo L, Moulin M, Haertlein M, Meilleur F, Christianson DW. Expression, purification, assay, and crystal structure of perdeuterated human arginase I. Arch. Biochem. Biophys. 465 2007 82-9 [PubMed: 17562323] http://dx.doi.org/10.1016/j.abb.2007.04.036
	Zakharian TY, Di Costanzo L, Christianson DW. Synthesis of (2S)-2-amino-7,8-epoxyoctanoic acid and structure of its metal-bridging complex with human arginase I. Org. Biomol. Chem. 6 2008 3240-3 [PubMed: 18802628] http://dx.doi.org/10.1039/b811797g

InterPro 24.0