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P46637 (ARGI1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginase 1, mitochondrial

EC=3.5.3.1
Alternative name(s):
Arginine amidohydrolase 1
Gene names
Name:ARGAH1
Ordered Locus Names:At4g08900
ORF Names:T3H13.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the hydrolysis of L-arginine to urea and L-ornithine. The latter can be utilized in the urea cycle or as a precursor for the synthesis of both polyamines and proline By similarity.

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.

Subcellular location

Mitochondrion Ref.6.

Tissue specificity

Expressed in vasculature of roots, root tips, cotyledons, leaves, cauline leaves, stems, sepals and pollen. Ref.5 Ref.6

Disruption phenotype

Increased formation of lateral and adventitious roots and increased production of NO in roots. Ref.6

Sequence similarities

Belongs to the arginase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion Potential
Chain25 – 342318Arginase 1, mitochondrial
PRO_0000173703

Regions

Region187 – 1915Substrate binding By similarity
Region195 – 1973Substrate binding By similarity

Sites

Metal binding1611Manganese 1 By similarity
Metal binding1851Manganese 1 By similarity
Metal binding1851Manganese 2 By similarity
Metal binding1871Manganese 2 By similarity
Metal binding1891Manganese 1 By similarity
Metal binding2701Manganese 1 By similarity
Metal binding2701Manganese 2 By similarity
Metal binding2721Manganese 2 By similarity
Binding site2261Substrate By similarity
Binding site3131Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P46637 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: B656635BB51DCD3F

FASTA34237,345
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Analysis of Arabidopsis arginase gene transcription patterns indicates specific biological functions for recently diverged paralogs."
Brownfield D.L., Todd C.D., Deyholos M.K.
Plant Mol. Biol. 67:429-440(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Arginase-negative mutants of Arabidopsis exhibit increased nitric oxide signaling in root development."
Flores T., Todd C.D., Tovar-Mendez A., Dhanoa P.K., Correa-Aragunde N., Hoyos M.E., Brownfield D.M., Mullen R.T., Lamattina L., Polacco J.C.
Plant Physiol. 147:1936-1946(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15019 mRNA. Translation: AAA85816.1.
AF128396 Genomic DNA. Translation: AAD17369.1.
AL161513 Genomic DNA. Translation: CAB78014.1.
CP002687 Genomic DNA. Translation: AEE82694.1.
AY052276 mRNA. Translation: AAK96469.1.
AY061914 mRNA. Translation: AAL31241.1.
PIRF85089.
RefSeqNP_192629.1. NM_116959.3.
UniGeneAt.1554.

3D structure databases

ProteinModelPortalP46637.
SMRP46637. Positions 66-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid11767. 1 interaction.
IntActP46637. 1 interaction.
STRING3702.AT4G08900.1-P.

Proteomic databases

PaxDbP46637.
PRIDEP46637.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G08900.1; AT4G08900.1; AT4G08900.
GeneID826468.
KEGGath:AT4G08900.

Organism-specific databases

TAIRAT4G08900.

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204320.
InParanoidP46637.
KOK01476.
OMAFVCLDAH.
PhylomeDBP46637.
ProtClustDBPLN02615.

Enzyme and pathway databases

BioCycARA:AT4G08900-MONOMER.
MetaCyc:AT4G08900-MONOMER.
UniPathwayUPA00158; UER00270.

Gene expression databases

GenevestigatorP46637.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP46637.

Entry information

Entry nameARGI1_ARATH
AccessionPrimary (citable) accession number: P46637
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names