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P46637

- ARGI1_ARATH

UniProt

P46637 - ARGI1_ARATH

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
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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

    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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Arginine metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT4G08900-MONOMER.
    MetaCyc:AT4G08900-MONOMER.
    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-SubCell

    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

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    MSRIIGRKGI NYIHRLNSAS FTSVSASSIE KGQNRVIDAS LTLIRERAKL    50
    KGELVRLLGG AKASTSLLGV PLGHNSSFLQ GPAFAPPRIR EAIWCGSTNS 100
    ATEEGKELKD PRVLTDVGDV PVQEIRDCGV DDDRLMNVIS ESVKLVMEEE 150
    PLRPLVLGGD HSISYPVVRA VSEKLGGPVD ILHLDAHPDI YDCFEGNKYS 200
    HASSFARIME GGYARRLLQV GIRSINQEGR EQGKRFGVEQ YEMRTFSKDR 250
    PMLENLKLGE GVKGVYISID VDCLDPAFAP GVSHIEPGGL SFRDVLNILH 300
    NLQADVVGAD VVEFNPQRDT VDGMTAMVAA KLVRELAAKI SK 342
    Length:342
    Mass (Da):37,345
    Last modified:November 1, 1995 - v1
    Checksum:iB656635BB51DCD3F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.

    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

    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: October 1, 2014
    This is version 110 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