URH2_ARATH
ID URH2_ARATH Reviewed; 322 AA.
AC Q8LAC4; B3H6Y7; Q9SYK3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable uridine nucleosidase 2 {ECO:0000303|PubMed:19293370};
DE EC=3.2.2.3 {ECO:0000250|UniProtKB:Q9SJM7};
DE AltName: Full=Inosine nucleosidase {ECO:0000303|PubMed:21235647};
DE EC=3.2.2.2 {ECO:0000269|PubMed:21235647};
DE AltName: Full=Nucleoside hydrolase 2 {ECO:0000303|PubMed:21235647};
DE AltName: Full=Uridine ribohydrolase 2 {ECO:0000303|PubMed:19293370};
DE AltName: Full=Xanthosine nucleosidase {ECO:0000303|PubMed:30787180};
DE EC=3.2.2.- {ECO:0000269|PubMed:30787180};
GN Name=URH2 {ECO:0000303|PubMed:19293370};
GN Synonyms=NSH2 {ECO:0000303|PubMed:21235647};
GN OrderedLocusNames=At1g05620 {ECO:0000312|Araport:AT1G05620};
GN ORFNames=F3F20.7 {ECO:0000312|EMBL:AAD30614.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=19293370; DOI=10.1105/tpc.108.062612;
RA Jung B., Florchinger M., Kunz H.H., Traub M., Wartenberg R., Jeblick W.,
RA Neuhaus H.E., Mohlmann T.;
RT "Uridine-ribohydrolase is a key regulator in the uridine degradation
RT pathway of Arabidopsis.";
RL Plant Cell 21:876-891(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21599668; DOI=10.1111/j.1469-8137.2011.03711.x;
RA Riegler H., Geserick C., Zrenner R.;
RT "Arabidopsis thaliana nucleosidase mutants provide new insights into
RT nucleoside degradation.";
RL New Phytol. 191:349-359(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION BY
RP SENESCENCE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21235647; DOI=10.1111/j.1365-313x.2010.04455.x;
RA Jung B., Hoffmann C., Moehlmann T.;
RT "Arabidopsis nucleoside hydrolases involved in intracellular and
RT extracellular degradation of purines.";
RL Plant J. 65:703-711(2011).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, SUBUNIT, INTERACTION WITH URH1, MUTAGENESIS OF ASP-14, AND
RP ACTIVE SITE.
RC STRAIN=cv. Columbia;
RX PubMed=30787180; DOI=10.1105/tpc.18.00899;
RA Baccolini C., Witte C.-P.;
RT "AMP and GMP catabolism in Arabidopsis converge on xanthosine, which is
RT degraded by a nucleoside hydrolase heterocomplex.";
RL Plant Cell 31:734-751(2019).
CC -!- FUNCTION: Involved in pyrimidine breakdown, especially in response to
CC dark stress (PubMed:21599668, PubMed:30787180). In the presence of
CC URH1, exhibits efficient inosine and xanthosine hydrolytic activities
CC (PubMed:21599668, PubMed:30787180). Support inosine breakdown
CC especially during the late phase of senescence (PubMed:21235647).
CC {ECO:0000269|PubMed:21235647, ECO:0000269|PubMed:21599668,
CC ECO:0000269|PubMed:30787180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + uridine = D-ribose + uracil; Xref=Rhea:RHEA:15577,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:47013; EC=3.2.2.3;
CC Evidence={ECO:0000250|UniProtKB:Q9SJM7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + inosine = D-ribose + hypoxanthine; Xref=Rhea:RHEA:16657,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596,
CC ChEBI:CHEBI:47013; EC=3.2.2.2;
CC Evidence={ECO:0000269|PubMed:21235647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + xanthosine = D-ribose + xanthine; Xref=Rhea:RHEA:27994,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17712, ChEBI:CHEBI:18107,
CC ChEBI:CHEBI:47013; Evidence={ECO:0000269|PubMed:30787180};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for xanthosine (when in complex with URH2)
CC {ECO:0000269|PubMed:30787180};
CC KM=4.30 mM for uridine (when in complex with URH2)
CC {ECO:0000269|PubMed:30787180};
CC KM=0.60 mM for inosine (when in complex with URH2)
CC {ECO:0000269|PubMed:30787180};
CC Note=kcat is 23.3 sec(-1) with xanthosine as substrate (when in
CC complex with URH2) (PubMed:30787180). kcat is 55.3 sec(-1) with
CC uridine as substrate (when in complex with URH2) (PubMed:30787180).
CC kcat is 42.3 sec(-1) with inosine as substrate (when in complex with
CC URH2) (PubMed:30787180). {ECO:0000269|PubMed:30787180};
CC -!- SUBUNIT: Component of the NSH heterocomplex made of URH1/NSH1 and
CC URH2/NSH2 which exhibits strong xanthosine nucleosidase activity
CC (PubMed:30787180). Interacts with URH1 (PubMed:30787180).
CC {ECO:0000269|PubMed:30787180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21235647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LAC4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LAC4-2; Sequence=VSP_039276;
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings and flowers.
CC {ECO:0000269|PubMed:30787180}.
CC -!- INDUCTION: Accumulates during senescence.
CC {ECO:0000269|PubMed:21235647}.
CC -!- DISRUPTION PHENOTYPE: Normal seedling germination and plant growth and
CC development in standard conditions (PubMed:21599668). No abnormal
CC levels of nucleoside intermediates (PubMed:21599668). The roots of the
CC double mutant urh1 urh2 accumulates strong levels of xanthosine
CC (PubMed:21599668, PubMed:30787180). {ECO:0000269|PubMed:21599668,
CC ECO:0000269|PubMed:30787180}.
CC -!- SIMILARITY: Belongs to the IUNH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007153; AAD30614.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27866.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27867.1; -; Genomic_DNA.
DR EMBL; BT002049; AAN72060.1; -; mRNA.
DR EMBL; BT008720; AAP42733.1; -; mRNA.
DR EMBL; AY087913; AAM65464.1; -; mRNA.
DR PIR; C86190; C86190.
DR RefSeq; NP_001117234.1; NM_001123762.2. [Q8LAC4-2]
DR RefSeq; NP_563745.1; NM_100442.5. [Q8LAC4-1]
DR AlphaFoldDB; Q8LAC4; -.
DR SMR; Q8LAC4; -.
DR BioGRID; 22310; 1.
DR STRING; 3702.AT1G05620.1; -.
DR PaxDb; Q8LAC4; -.
DR PRIDE; Q8LAC4; -.
DR ProteomicsDB; 228634; -. [Q8LAC4-1]
DR EnsemblPlants; AT1G05620.1; AT1G05620.1; AT1G05620. [Q8LAC4-1]
DR EnsemblPlants; AT1G05620.2; AT1G05620.2; AT1G05620. [Q8LAC4-2]
DR GeneID; 837068; -.
DR Gramene; AT1G05620.1; AT1G05620.1; AT1G05620. [Q8LAC4-1]
DR Gramene; AT1G05620.2; AT1G05620.2; AT1G05620. [Q8LAC4-2]
DR KEGG; ath:AT1G05620; -.
DR Araport; AT1G05620; -.
DR TAIR; locus:2032008; AT1G05620.
DR eggNOG; KOG2938; Eukaryota.
DR HOGENOM; CLU_036838_2_1_1; -.
DR InParanoid; Q8LAC4; -.
DR OMA; HAPDIHG; -.
DR OrthoDB; 824591at2759; -.
DR PhylomeDB; Q8LAC4; -.
DR PRO; PR:Q8LAC4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LAC4; baseline and differential.
DR Genevisible; Q8LAC4; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0047724; F:inosine nucleosidase activity; IMP:TAIR.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0008477; F:purine nucleosidase activity; IDA:TAIR.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:TAIR.
DR GO; GO:0045437; F:uridine nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0072585; F:xanthosine nucleotidase activity; IEA:RHEA.
DR GO; GO:0006148; P:inosine catabolic process; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IEP:TAIR.
DR GO; GO:0006152; P:purine nucleoside catabolic process; IBA:GO_Central.
DR Gene3D; 3.90.245.10; -; 1.
DR InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR InterPro; IPR023186; IUNH.
DR InterPro; IPR036452; Ribo_hydro-like.
DR PANTHER; PTHR12304; PTHR12304; 1.
DR Pfam; PF01156; IU_nuc_hydro; 1.
DR SUPFAM; SSF53590; SSF53590; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..322
FT /note="Probable uridine nucleosidase 2"
FT /id="PRO_0000394503"
FT ACT_SITE 14
FT /evidence="ECO:0000269|PubMed:30787180"
FT ACT_SITE 246
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..20
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039276"
FT MUTAGEN 14
FT /note="D->A: Abrogated hydrolase activity."
FT /evidence="ECO:0000269|PubMed:30787180"
SQ SEQUENCE 322 AA; 34668 MW; BB13A4C2004C39AF CRC64;
MAIGDRKKII IDTDPGIDDA MAIFVALNSP EVDVIGLTTI FGNVYTTLAT RNALHLLEVA
GRTDIPVAEG THKTFLNDTK LRIADFVHGK DGLGNQNFPP PKGKPIEKSG PEFLVEQAKL
CPGEITVVAL GPLTNLALAV QLDPEFSKNV GQIVLLGGAF AVNGNVNPAS EANIFGDPEA
ADIVFTCGAD IIAVGINVTH QVIMTADDKD KLASSKGKLA QYLCKILDVY YDYHLTAYEI
KGVYLHDPAT ILAAFLPSLF TYTEGVARVQ TSGITRGLTL LYNNLKRFEE ANEWSDKPTV
KVAVTVDAPA VVKLIMDRLM ES
