ARGI1_ARATH
ID ARGI1_ARATH Reviewed; 342 AA.
AC P46637;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Arginase 1, mitochondrial {ECO:0000305};
DE EC=3.5.3.1 {ECO:0000305|PubMed:32754173};
DE AltName: Full=Agmatinase ARGAH1 {ECO:0000305};
DE EC=3.5.3.11 {ECO:0000305|PubMed:28716421};
DE AltName: Full=Arginine amidohydrolase 1 {ECO:0000305};
DE Short=AtARGAH1 {ECO:0000303|PubMed:32754173};
DE Flags: Precursor;
GN Name=ARGAH1 {ECO:0000303|PubMed:32754173}; OrderedLocusNames=At4g08900;
GN ORFNames=T3H13.7;
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 [MRNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7770544; DOI=10.1104/pp.107.4.1479;
RA Krumpelman P.M., Freyermuth S.K., Cannon J.F., Fink G.R., Polacco J.C.;
RT "Nucleotide sequence of Arabidopsis thaliana arginase expressed in yeast.";
RL Plant Physiol. 107:1479-1480(1995).
RN [2]
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 [3]
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 [4]
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 [5]
RP TISSUE SPECIFICITY.
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP THR-22.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 25-342 IN COMPLEX WITH ORNITHINE
RP AND MANGANESE IONS, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=32754173; DOI=10.3389/fpls.2020.00987;
RA Sekula B.;
RT "The neighboring subunit is engaged to stabilize the substrate in the
RT active site of plant arginases.";
RL Front. Plant Sci. 11:987-987(2020).
CC -!- FUNCTION: Catalyzes the hydrolysis of L-arginine to urea and L-
CC ornithine (Probable). The latter can be utilized in the urea cycle or
CC as a precursor for the synthesis of both polyamines and proline
CC (Probable). Possesses agmatinase activity. Catalyzes the formation of
CC putrescine from agmatine (PubMed:28716421).
CC {ECO:0000269|PubMed:28716421, ECO:0000305|PubMed:32754173}.
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:0000305|PubMed:32754173};
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:0000305|PubMed:28716421};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742,
CC ECO:0000269|PubMed:32754173};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742, ECO:0000269|PubMed:32754173};
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 -!- SUBUNIT: Forms homohexamers. {ECO:0000269|PubMed:32754173}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18567826,
CC ECO:0000305|PubMed:25732537}.
CC -!- TISSUE SPECIFICITY: Expressed in vasculature of roots, root tips,
CC cotyledons, leaves, cauline leaves, stems, sepals and pollen.
CC {ECO:0000269|PubMed:18425591, ECO:0000269|PubMed:18567826}.
CC -!- DISRUPTION PHENOTYPE: Increased formation of lateral and adventitious
CC roots and increased production of NO in roots.
CC {ECO:0000269|PubMed:18567826}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; U15019; AAA85816.1; -; mRNA.
DR EMBL; AF128396; AAD17369.1; -; Genomic_DNA.
DR EMBL; AL161513; CAB78014.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82694.1; -; Genomic_DNA.
DR EMBL; AY052276; AAK96469.1; -; mRNA.
DR EMBL; AY061914; AAL31241.1; -; mRNA.
DR PIR; F85089; F85089.
DR RefSeq; NP_192629.1; NM_116959.4.
DR PDB; 6VSU; X-ray; 2.25 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=25-342.
DR PDBsum; 6VSU; -.
DR AlphaFoldDB; P46637; -.
DR SMR; P46637; -.
DR BioGRID; 11767; 2.
DR IntAct; P46637; 1.
DR STRING; 3702.AT4G08900.1; -.
DR MetOSite; P46637; -.
DR PaxDb; P46637; -.
DR PRIDE; P46637; -.
DR ProteomicsDB; 246832; -.
DR EnsemblPlants; AT4G08900.1; AT4G08900.1; AT4G08900.
DR GeneID; 826468; -.
DR Gramene; AT4G08900.1; AT4G08900.1; AT4G08900.
DR KEGG; ath:AT4G08900; -.
DR Araport; AT4G08900; -.
DR TAIR; locus:2138718; AT4G08900.
DR eggNOG; KOG2964; Eukaryota.
DR HOGENOM; CLU_039478_3_0_1; -.
DR InParanoid; P46637; -.
DR OMA; CIDAGFV; -.
DR OrthoDB; 921352at2759; -.
DR PhylomeDB; P46637; -.
DR BioCyc; ARA:AT4G08900-MON; -.
DR BioCyc; MetaCyc:AT4G08900-MON; -.
DR UniPathway; UPA00158; UER00270.
DR UniPathway; UPA00534; UER00287.
DR PRO; PR:P46637; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P46637; baseline and differential.
DR Genevisible; P46637; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0008783; F:agmatinase activity; IDA:UniProtKB.
DR GO; GO:0004053; F:arginase activity; IMP:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0006527; P:arginine catabolic process; IGI:TAIR.
DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IDA:UniProtKB.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR SUPFAM; SSF52768; SSF52768; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW Mitochondrion; Putrescine biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 23..342
FT /note="Arginase 1, mitochondrial"
FT /id="PRO_0000173703"
FT BINDING 77
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:32754173"
FT BINDING 96..99
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:32754173"
FT BINDING 161
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:32754173"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:32754173"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:32754173"
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 ECO:0000269|PubMed:32754173"
FT BINDING 189..191
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:32754173"
FT BINDING 189
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:32754173"
FT BINDING 195..197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 224
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|PubMed:32754173"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:32754173"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742,
FT ECO:0000269|PubMed:32754173"
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 ECO:0000269|PubMed:32754173"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:32754173"
FT HELIX 29..57
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:6VSU"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6VSU"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:6VSU"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6VSU"
FT HELIX 324..340
FT /evidence="ECO:0007829|PDB:6VSU"
SQ SEQUENCE 342 AA; 37345 MW; B656635BB51DCD3F CRC64;
MSRIIGRKGI NYIHRLNSAS FTSVSASSIE KGQNRVIDAS LTLIRERAKL KGELVRLLGG
AKASTSLLGV PLGHNSSFLQ GPAFAPPRIR EAIWCGSTNS ATEEGKELKD PRVLTDVGDV
PVQEIRDCGV DDDRLMNVIS ESVKLVMEEE PLRPLVLGGD HSISYPVVRA VSEKLGGPVD
ILHLDAHPDI YDCFEGNKYS HASSFARIME GGYARRLLQV GIRSINQEGR EQGKRFGVEQ
YEMRTFSKDR PMLENLKLGE GVKGVYISID VDCLDPAFAP GVSHIEPGGL SFRDVLNILH
NLQADVVGAD VVEFNPQRDT VDGMTAMVAA KLVRELAAKI SK
