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P46637

- ARGI1_ARATH

UniProt

P46637 - ARGI1_ARATH

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Protein

Arginase 1, mitochondrial

Gene

ARGAH1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.

Cofactori

Mn2+PROSITE-ProRule annotationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi161 – 1611Manganese 1PROSITE-ProRule annotation
Metal bindingi185 – 1851Manganese 1PROSITE-ProRule annotation
Metal bindingi185 – 1851Manganese 2PROSITE-ProRule annotation
Metal bindingi187 – 1871Manganese 2PROSITE-ProRule annotation
Metal bindingi189 – 1891Manganese 1PROSITE-ProRule annotation
Binding sitei226 – 2261SubstrateBy similarity
Metal bindingi270 – 2701Manganese 1PROSITE-ProRule annotation
Metal bindingi270 – 2701Manganese 2PROSITE-ProRule annotation
Metal bindingi272 – 2721Manganese 2PROSITE-ProRule annotation
Binding sitei313 – 3131SubstrateBy similarity

GO - Molecular functioni

  1. arginase activity Source: TAIR
  2. cobalt ion binding Source: TAIR

GO - Biological processi

  1. arginine catabolic process Source: TAIR
  2. defense response to bacterium Source: TAIR
  3. urea cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G08900-MONOMER.
MetaCyc:AT4G08900-MONOMER.
ReactomeiREACT_232294. Agmatine biosynthesis.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase 1, mitochondrial (EC:3.5.3.1)
Alternative name(s):
Arginine amidohydrolase 1
Gene namesi
Name:ARGAH1
Ordered Locus Names:At4g08900
ORF Names:T3H13.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G08900.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Increased formation of lateral and adventitious roots and increased production of NO in roots.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionSequence AnalysisAdd
BLAST
Chaini25 – 342318Arginase 1, mitochondrialPRO_0000173703Add
BLAST

Proteomic databases

PaxDbiP46637.
PRIDEiP46637.

Expressioni

Tissue specificityi

Expressed in vasculature of roots, root tips, cotyledons, leaves, cauline leaves, stems, sepals and pollen.2 Publications

Gene expression databases

GenevestigatoriP46637.

Interactioni

Protein-protein interaction databases

BioGridi11767. 2 interactions.
IntActiP46637. 1 interaction.
STRINGi3702.AT4G08900.1-P.

Structurei

3D structure databases

ProteinModelPortaliP46637.
SMRiP46637. Positions 66-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 1915Substrate bindingBy similarity
Regioni195 – 1973Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0010.
HOGENOMiHOG000204320.
InParanoidiP46637.
KOiK01476.
OMAiHNLQGDV.
PhylomeDBiP46637.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46637-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRIIGRKGI NYIHRLNSAS FTSVSASSIE KGQNRVIDAS LTLIRERAKL
60 70 80 90 100
KGELVRLLGG AKASTSLLGV PLGHNSSFLQ GPAFAPPRIR EAIWCGSTNS
110 120 130 140 150
ATEEGKELKD PRVLTDVGDV PVQEIRDCGV DDDRLMNVIS ESVKLVMEEE
160 170 180 190 200
PLRPLVLGGD HSISYPVVRA VSEKLGGPVD ILHLDAHPDI YDCFEGNKYS
210 220 230 240 250
HASSFARIME GGYARRLLQV GIRSINQEGR EQGKRFGVEQ YEMRTFSKDR
260 270 280 290 300
PMLENLKLGE GVKGVYISID VDCLDPAFAP GVSHIEPGGL SFRDVLNILH
310 320 330 340
NLQADVVGAD VVEFNPQRDT VDGMTAMVAA KLVRELAAKI SK
Length:342
Mass (Da):37,345
Last modified:November 1, 1995 - v1
Checksum:iB656635BB51DCD3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiF85089.
RefSeqiNP_192629.1. NM_116959.3.
UniGeneiAt.1554.

Genome annotation databases

EnsemblPlantsiAT4G08900.1; AT4G08900.1; AT4G08900.
GeneIDi826468.
KEGGiath:AT4G08900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi F85089.
RefSeqi NP_192629.1. NM_116959.3.
UniGenei At.1554.

3D structure databases

ProteinModelPortali P46637.
SMRi P46637. Positions 66-336.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 11767. 2 interactions.
IntActi P46637. 1 interaction.
STRINGi 3702.AT4G08900.1-P.

Proteomic databases

PaxDbi P46637.
PRIDEi P46637.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G08900.1 ; AT4G08900.1 ; AT4G08900 .
GeneIDi 826468.
KEGGi ath:AT4G08900.

Organism-specific databases

TAIRi AT4G08900.

Phylogenomic databases

eggNOGi COG0010.
HOGENOMi HOG000204320.
InParanoidi P46637.
KOi K01476.
OMAi HNLQGDV.
PhylomeDBi P46637.

Enzyme and pathway databases

UniPathwayi UPA00158 ; UER00270 .
BioCyci ARA:AT4G08900-MONOMER.
MetaCyc:AT4G08900-MONOMER.
Reactomei REACT_232294. Agmatine biosynthesis.

Miscellaneous databases

PROi P46637.

Gene expression databases

Genevestigatori P46637.

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
PROSITEi PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiARGI1_ARATH
AccessioniPrimary (citable) accession number: P46637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3