Reviewed, UniProtKB/Swiss-Prot P46637 (ARGI1_ARATH)

Names and origin

Protein names

Recommended name:
    Arginase
    EC=3.5.3.1

Gene names

Ordered Locus Names:	At4g08900
ORF Names:	T3H13.7

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	342 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	L-arginine + H2O = L-ornithine + urea.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Pathway	Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
Sequence similarities	Belongs to the arginase family.

Ontologies

Keywords
Biological process	Arginine metabolism
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process Ref.1 Inferred from genetic interaction. Source: TAIR defense response to bacterium Inferred from expression pattern. Source: TAIR
Cellular component	chloroplast Inferred from direct assay. Source: TAIR
Molecular function	arginase activity Ref.1 Inferred from mutant phenotype. Source: TAIR manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 342	342	Arginase		PRO_0000173703
Regions
	Region	187 – 191	5	Substrate binding Potential
	Region	195 – 197	3	Substrate binding Potential
Sites
	Metal binding	161	1	Manganese 1 By similarity
	Metal binding	185	1	Manganese 1 By similarity
	Metal binding	185	1	Manganese 2 By similarity
	Metal binding	187	1	Manganese 2 By similarity
	Metal binding	189	1	Manganese 1 By similarity
	Metal binding	270	1	Manganese 1 By similarity
	Metal binding	270	1	Manganese 2 By similarity
	Metal binding	272	1	Manganese 2 By similarity
	Binding site	226	1	Substrate Potential
	Binding site	313	1	Substrate Potential

Sequences

	Sequence		Length	Mass (Da)
	P46637-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: B656635BB51DCD3F	FASTA	342	37,345
	10 20 30 40 50 60 MSRIIGRKGI NYIHRLNSAS FTSVSASSIE KGQNRVIDAS LTLIRERAKL KGELVRLLGG 70 80 90 100 110 120 AKASTSLLGV PLGHNSSFLQ GPAFAPPRIR EAIWCGSTNS ATEEGKELKD PRVLTDVGDV 130 140 150 160 170 180 PVQEIRDCGV DDDRLMNVIS ESVKLVMEEE PLRPLVLGGD HSISYPVVRA VSEKLGGPVD 190 200 210 220 230 240 ILHLDAHPDI YDCFEGNKYS HASSFARIME GGYARRLLQV GIRSINQEGR EQGKRFGVEQ 250 260 270 280 290 300 YEMRTFSKDR PMLENLKLGE GVKGVYISID VDCLDPAFAP GVSHIEPGGL SFRDVLNILH 310 320 330 340 NLQADVVGAD VVEFNPQRDT VDGMTAMVAA KLVRELAAKI SK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Arabidopsis thaliana arginase expressed in yeast." Krumpelman P.M., Freyermuth S.K., Cannon J.F., Fink G.R., Polacco J.C. Plant Physiol. 107:1479-1480(1995) [PubMed: 7770544] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U15019 mRNA. Translation: AAA85816.1. AF128396 Genomic DNA. Translation: AAD17369.1. AL161513 Genomic DNA. Translation: CAB78014.1. AY052276 mRNA. Translation: AAK96469.1. AY061914 mRNA. Translation: AAL31241.1.
IPI	IPI00517952.
PIR	F85089.
RefSeq	NP_192629.1.
UniGene	At.1554
3D structure databases
HSSP	HSSP built from PDB template 1GQ6 based on UniProtKB P37819.
ModBase	Search...
Protein-protein interaction databases
STRING	P46637.
Proteomic databases
PRIDE	P46637.
Genome annotation databases
GeneID	826468.
GenomeReviews	Gene locus AT4G08900 in contig CT486007_GR.
KEGG	ath:AT4G08900.
NMPDR	fig|3702.1.peg.18546.
Organism-specific databases
TAIR	At4g08900.
Phylogenomic databases
OMA	MGGEHLV.
Enzyme and pathway databases
BRENDA	3.5.3.1. 302.
Gene expression databases
Genevestigator	P46637.
GermOnline	AT4G08900. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR006035. Ureohydrolase. [Graphical view]
Gene3D	G3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHER	PTHR11358. Ureohydrolase. 1 hit.
Pfam	PF00491. Arginase. 1 hit. [Graphical view]
PROSITE	PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGI1_ARATH

Accession

Primary (citable) accession number: P46637

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)