ACR21_ORYSJ
ID ACR21_ORYSJ Reviewed; 160 AA.
AC Q336V5; A0A0P0XWU2; Q9AV34;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Arsenate reductase 2.1;
DE Short=OsACR2.1;
DE EC=1.20.4.1;
DE AltName: Full=Dual specificity phosphatase CDC25.1;
DE AltName: Full=Sulfurtransferase 20;
DE Short=OsStr20;
GN Name=ACR2.1; Synonyms=CDC25.1, STR20;
GN OrderedLocusNames=Os10g0545700, LOC_Os10g39860;
GN ORFNames=OsJ_32347, OSJNBa0001O14.6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 3-160, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND MUTAGENESIS OF CYS-94.
RC TISSUE=Root;
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 [8]
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=12.2 mM for arsenate {ECO:0000269|PubMed:17388894};
CC Vmax=117 nmol/min/mg enzyme towards arsenate
CC {ECO:0000269|PubMed:17388894};
CC -!- INDUCTION: By arsenate. {ECO:0000269|PubMed:17388894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK20061.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAX54896.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE51343.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC025783; AAK20061.1; ALT_INIT; Genomic_DNA.
DR EMBL; DP000086; ABB47952.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF27125.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11901.1; -; Genomic_DNA.
DR EMBL; CM000147; EEE51343.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK074009; BAG93758.1; -; mRNA.
DR EMBL; AK104025; BAG96379.1; -; mRNA.
DR EMBL; AY860059; AAX54896.1; ALT_INIT; mRNA.
DR RefSeq; XP_015612765.1; XM_015757279.1.
DR AlphaFoldDB; Q336V5; -.
DR SMR; Q336V5; -.
DR STRING; 4530.OS10T0545700-02; -.
DR PRIDE; Q336V5; -.
DR EnsemblPlants; Os10t0545700-02; Os10t0545700-02; Os10g0545700.
DR EnsemblPlants; Os10t0545700-03; Os10t0545700-03; Os10g0545700.
DR GeneID; 4349283; -.
DR Gramene; Os10t0545700-02; Os10t0545700-02; Os10g0545700.
DR Gramene; Os10t0545700-03; Os10t0545700-03; Os10g0545700.
DR KEGG; osa:4349283; -.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_107716_2_0_1; -.
DR InParanoid; Q336V5; -.
DR OMA; PVCRCTN; -.
DR OrthoDB; 1513881at2759; -.
DR BRENDA; 1.20.99.1; 4460.
DR SABIO-RK; Q336V5; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q336V5; baseline and differential.
DR Genevisible; Q336V5; 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 SMART; SM00450; RHOD; 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..160
FT /note="Arsenate reductase 2.1"
FT /id="PRO_0000416540"
FT DOMAIN 42..143
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 94
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT MUTAGEN 94
FT /note="C->S: Loss of phosphatase activity. Decreases
FT arsenate reductase catalytic efficiency 14-fold."
FT /evidence="ECO:0000269|PubMed:17388894"
SQ SEQUENCE 160 AA; 17705 MW; 3A31CBB109FFA25E CRC64;
MCRFLISTPF SRRRGERKAE AGRMARSVSY VSAAKLLAMA RSNPRVAIID VRDEERSYQA
HIGGSHHFSS RSFAARLPEL ARATGDKDTV VFHCALSKVR GPSCAKMFSD YLSETKEESG
TKNIMVLERG FNGWELSGQP VCRCTDAPCK GTCSPEEPEL
