ARGI2_ARATH
ID ARGI2_ARATH Reviewed; 344 AA.
AC Q9ZPF5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Arginase 2, chloroplastic/mitochondrial;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
DE AltName: Full=Agmatinase ARGAH2 {ECO:0000305};
DE EC=3.5.3.11 {ECO:0000269|PubMed:28716421};
DE AltName: Full=Arginine amidohydrolase 2;
DE Flags: Precursor;
GN Name=ARGAH2; OrderedLocusNames=At4g08870; ORFNames=T3H13.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION BY METHYL JASMONATE.
RX PubMed=18425591; DOI=10.1007/s11103-008-9336-2;
RA Brownfield D.L., Todd C.D., Deyholos M.K.;
RT "Analysis of Arabidopsis arginase gene transcription patterns indicates
RT specific biological functions for recently diverged paralogs.";
RL Plant Mol. Biol. 67:429-440(2008).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18567826; DOI=10.1104/pp.108.121459;
RA Flores T., Todd C.D., Tovar-Mendez A., Dhanoa P.K., Correa-Aragunde N.,
RA Hoyos M.E., Brownfield D.M., Mullen R.T., Lamattina L., Polacco J.C.;
RT "Arginase-negative mutants of Arabidopsis exhibit increased nitric oxide
RT signaling in root development.";
RL Plant Physiol. 147:1936-1946(2008).
RN [6]
RP INDUCTION.
RX PubMed=22188168; DOI=10.1111/j.1438-8677.2011.00520.x;
RA Brauc S., De Vooght E., Claeys M., Geuns J.M., Hoefte M., Angenon G.;
RT "Overexpression of arginase in Arabidopsis thaliana influences defence
RT responses against Botrytis cinerea.";
RL Plant Biol. 14:39-45(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=28716421; DOI=10.1016/j.plantsci.2017.05.011;
RA Patel J., Ariyaratne M., Ahmed S., Ge L., Phuntumart V., Kalinoski A.,
RA Morris P.F.;
RT "Dual functioning of plant arginases provides a third route for putrescine
RT synthesis.";
RL Plant Sci. 262:62-73(2017).
CC -!- FUNCTION: Catalyzes the hydrolysis of L-arginine to urea and L-
CC ornithine. The latter can be utilized in the urea cycle or as a
CC precursor for the synthesis of both polyamines and proline (By
CC similarity). Possesses agmatinase activity. Catalyzes the formation of
CC putrescine from agmatine (PubMed:28716421).
CC {ECO:0000250|UniProtKB:P05089, ECO:0000269|PubMed:28716421}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911; EC=3.5.3.1;
CC Evidence={ECO:0000250|UniProtKB:P05089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145,
CC ChEBI:CHEBI:326268; EC=3.5.3.11;
CC Evidence={ECO:0000269|PubMed:28716421};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=72.6 uM for agmatine {ECO:0000269|PubMed:28716421};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from agmatine: step 1/1.
CC {ECO:0000305|PubMed:28716421}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18567826}.
CC Plastid, chloroplast {ECO:0000269|PubMed:28716421}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZPF5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in vasculature of roots, root tips,
CC leaves and cotyledons. {ECO:0000269|PubMed:18425591,
CC ECO:0000269|PubMed:18567826}.
CC -!- INDUCTION: By methyl jasmonate and infection with the fungal pathogen
CC B.cinerea. {ECO:0000269|PubMed:18425591, ECO:0000269|PubMed:22188168}.
CC -!- DISRUPTION PHENOTYPE: Increased formation of lateral and adventitious
CC roots and increased production of NO in roots.
CC {ECO:0000269|PubMed:18567826}.
CC -!- MISCELLANEOUS: Plants over-expressing ARGAH2 have decreased
CC susceptibility to the fungal pathogen B.cinerea.
CC {ECO:0000305|PubMed:22188168}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; AF128396; AAD17371.1; -; Genomic_DNA.
DR EMBL; AL161513; CAB78011.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82684.1; -; Genomic_DNA.
DR EMBL; BT003815; AAO41868.1; -; mRNA.
DR PIR; C85089; C85089.
DR RefSeq; NP_192626.1; NM_116956.4. [Q9ZPF5-1]
DR AlphaFoldDB; Q9ZPF5; -.
DR SMR; Q9ZPF5; -.
DR BioGRID; 11757; 1.
DR STRING; 3702.AT4G08870.1; -.
DR SWISS-2DPAGE; Q9ZPF5; -.
DR PaxDb; Q9ZPF5; -.
DR PRIDE; Q9ZPF5; -.
DR ProteomicsDB; 241057; -. [Q9ZPF5-1]
DR EnsemblPlants; AT4G08870.1; AT4G08870.1; AT4G08870. [Q9ZPF5-1]
DR GeneID; 826458; -.
DR Gramene; AT4G08870.1; AT4G08870.1; AT4G08870. [Q9ZPF5-1]
DR KEGG; ath:AT4G08870; -.
DR Araport; AT4G08870; -.
DR TAIR; locus:2138743; AT4G08870.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_3_0_1; -.
DR InParanoid; Q9ZPF5; -.
DR OMA; DQERITH; -.
DR PhylomeDB; Q9ZPF5; -.
DR UniPathway; UPA00158; UER00270.
DR UniPathway; UPA00534; UER00287.
DR PRO; PR:Q9ZPF5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZPF5; baseline and differential.
DR Genevisible; Q9ZPF5; AT.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0008783; F:agmatinase activity; IDA:TAIR.
DR GO; GO:0004053; F:arginase activity; IDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006591; P:ornithine metabolic process; IMP:TAIR.
DR GO; GO:0006560; P:proline metabolic process; IMP:TAIR.
DR GO; GO:0009446; P:putrescine biosynthetic process; IDA:TAIR.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IDA:UniProtKB.
DR GO; GO:0009445; P:putrescine metabolic process; IMP:TAIR.
DR GO; GO:0006570; P:tyrosine metabolic process; IMP:TAIR.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR SUPFAM; SSF52768; SSF52768; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Arginine metabolism; Chloroplast; Hydrolase;
KW Manganese; Metal-binding; Mitochondrion; Plastid; Putrescine biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..344
FT /note="Arginase 2, chloroplastic/mitochondrial"
FT /id="PRO_0000173704"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 189..193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 189
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 197..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 272
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
SQ SEQUENCE 344 AA; 37980 MW; FED95D31B1A2FEBE CRC64;
MWKIGQRGVP YFQRLIAAPF TTLRSLPTSL VETGQNRVID ASLTLIRERA KLKGELVRLI
GGAKATTALL GVPLGHNSSF LEGPALAPPH VREAIWCGST NSTTEEGKEL KDPRVLSDVG
DIPVQEIREM GVDDDRLMKV VSESVKLVME EEPLRPLVIG GDHSISYPVV RAVSEKLGGP
VDILHLDAHP DIYDRFEGNY YSHASSFARI MEGGYARRLL QVGIRSINKE GREQGKRFGV
EQYEMRTFSK DRQMLENLKL GEGVKGVYIS IDVDCLDPGF AHGVSHFEPG GLSFRDVLNI
LHNLQGDLVG ADVVEYNPQR DTADDMTAMV AAKFVRELAA KMSK
