ACR22_ORYSJ
ID ACR22_ORYSJ Reviewed; 130 AA.
AC Q10SX6; A0A0P0VS08; Q8H7Q4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Arsenate reductase 2.2;
DE Short=OsACR2.2;
DE EC=1.20.4.1;
DE AltName: Full=Dual specificity phosphatase CDC25.2;
DE AltName: Full=Sulfurtransferase 21;
DE Short=OsStr21;
GN Name=ACR2.2; Synonyms=CDC25.2, STR21;
GN OrderedLocusNames=Os03g0108000, LOC_Os03g01770;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND MUTAGENESIS OF CYS-70.
RC TISSUE=Shoot;
RX PubMed=17388894; DOI=10.1111/j.1469-8137.2007.02009.x;
RA Duan G.L., Zhou Y., Tong Y.P., Mukhopadhyay R., Rosen B.P., Zhu Y.G.;
RT "A CDC25 homologue from rice functions as an arsenate reductase.";
RL New Phytol. 174:311-321(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare; TISSUE=Shoot;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21821426; DOI=10.1016/j.plaphy.2011.07.010;
RA Guretzki S., Papenbrock J.;
RT "Characterization of the sulfurtransferase family from Oryza sativa L.";
RL Plant Physiol. Biochem. 49:1064-1070(2011).
CC -!- FUNCTION: Possesses arsenate reductase activity in vitro. Catalyzes the
CC reduction of arsenate [As(V)] to arsenite [As(III)]. May play a role in
CC arsenic retention in roots. {ECO:0000269|PubMed:17388894}.
CC -!- FUNCTION: Possesses phosphatase activity towards p-nitrophenyl
CC phosphate in vitro. {ECO:0000269|PubMed:17388894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[glutaredoxin]-dithiol + arsenate + glutathione + H(+) =
CC arsenite + glutathionyl-S-S-[glutaredoxin] + H2O;
CC Xref=Rhea:RHEA:22016, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:17668,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29242,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:48597, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:146199; EC=1.20.4.1;
CC Evidence={ECO:0000269|PubMed:17388894};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.2 mM for arsenate {ECO:0000269|PubMed:17388894};
CC Vmax=55 nmol/min/mg enzyme towards arsenate
CC {ECO:0000269|PubMed:17388894};
CC -!- INDUCTION: By arsenate. {ECO:0000269|PubMed:17388894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN62781.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY860058; AAX54895.1; -; mRNA.
DR EMBL; AC113930; AAN62781.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF93560.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF10612.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS81892.1; -; Genomic_DNA.
DR EMBL; AK102520; BAG95596.1; -; mRNA.
DR RefSeq; XP_015628914.1; XM_015773428.1.
DR AlphaFoldDB; Q10SX6; -.
DR SMR; Q10SX6; -.
DR STRING; 4530.OS03T0108000-01; -.
DR PaxDb; Q10SX6; -.
DR PRIDE; Q10SX6; -.
DR EnsemblPlants; Os03t0108000-01; Os03t0108000-01; Os03g0108000.
DR GeneID; 4331335; -.
DR Gramene; Os03t0108000-01; Os03t0108000-01; Os03g0108000.
DR KEGG; osa:4331335; -.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_107716_2_0_1; -.
DR InParanoid; Q10SX6; -.
DR OMA; CKDFRVA; -.
DR OrthoDB; 1513881at2759; -.
DR BRENDA; 1.20.99.1; 4460.
DR SABIO-RK; Q10SX6; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10SX6; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..130
FT /note="Arsenate reductase 2.2"
FT /id="PRO_0000416541"
FT DOMAIN 18..119
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 70
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT MUTAGEN 70
FT /note="C->S: Loss of phosphatase activity. Decreases
FT arsenate reductase catalytic efficiency 5-fold."
FT /evidence="ECO:0000269|PubMed:17388894"
SQ SEQUENCE 130 AA; 14364 MW; ECF1EDD577D1E207 CRC64;
MARGVSYVSA AQLVPMLRDP RIAVVDVRDE ERIYDAHIAG SHHYASDSFG ERLPELAQAT
KGKETLVFHC ALSKVRGPSC AQMYLDYLSE ADEDSDVKNI MVLERGFNGW ELSGRPVCRC
KDAPCKGVCS
