NUD25_ARATH
ID NUD25_ARATH Reviewed; 175 AA.
AC Q9C6Z2; Q0WMS9;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Nudix hydrolase 25 {ECO:0000303|PubMed:18345354, ECO:0000303|PubMed:18815383};
DE Short=AtNUDT25 {ECO:0000303|PubMed:18345354};
DE Short=AtNUDX25 {ECO:0000303|PubMed:18345354, ECO:0000303|PubMed:18815383};
DE EC=3.6.1.17 {ECO:0000269|PubMed:18345354};
DE AltName: Full=Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) {ECO:0000303|PubMed:18345354};
GN Name=NUDT25 {ECO:0000303|PubMed:18345354};
GN Synonyms=NUDX25 {ECO:0000303|PubMed:18345354, ECO:0000303|PubMed:18815383};
GN OrderedLocusNames=At1g30110 {ECO:0000312|Araport:AT1G30110};
GN ORFNames=T2H7.9 {ECO:0000312|EMBL:AAG50852.1};
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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-175.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=18815383; DOI=10.1104/pp.108.128413;
RA Ogawa T., Yoshimura K., Miyake H., Ishikawa K., Ito D., Tanabe N.,
RA Shigeoka S.;
RT "Molecular characterization of organelle-type Nudix hydrolases in
RT Arabidopsis.";
RL Plant Physiol. 148:1412-1424(2008).
RN [7]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=18345354;
RA Szurmak B., Wyslouch-Cieszynska A., Wszelaka-Rylik M., Bal W.,
RA Dobrzanska M.;
RT "A diadenosine 5',5''-P1P4 tetraphosphate (Ap4A) hydrolase from Arabidopsis
RT thaliana that is activated preferentially by Mn2+ ions.";
RL Acta Biochim. Pol. 55:151-160(2008).
CC -!- FUNCTION: Mediates the hydrolysis of diadenosine 5',5''-P(1)P(4)
CC tetraphosphate (Ap(4)A), a signaling molecule involved in regulation of
CC DNA replication and repair. {ECO:0000269|PubMed:18345354}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP +
CC 2 H(+); Xref=Rhea:RHEA:22484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57553, ChEBI:CHEBI:58115; EC=3.6.1.17;
CC Evidence={ECO:0000269|PubMed:18345354};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18345354};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. Active from pH 6.8 to 9.5.
CC {ECO:0000269|PubMed:18345354};
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18815383}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AC074176; AAG50852.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31179.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31180.1; -; Genomic_DNA.
DR EMBL; AY087445; AAM64991.1; -; mRNA.
DR EMBL; BT025530; ABF58948.1; -; mRNA.
DR EMBL; AK229734; BAF01571.1; -; mRNA.
DR PIR; B86425; B86425.
DR RefSeq; NP_001185114.1; NM_001198185.1.
DR RefSeq; NP_174303.1; NM_102750.5.
DR AlphaFoldDB; Q9C6Z2; -.
DR SMR; Q9C6Z2; -.
DR STRING; 3702.AT1G30110.1; -.
DR PaxDb; Q9C6Z2; -.
DR PRIDE; Q9C6Z2; -.
DR ProteomicsDB; 234941; -.
DR EnsemblPlants; AT1G30110.1; AT1G30110.1; AT1G30110.
DR EnsemblPlants; AT1G30110.2; AT1G30110.2; AT1G30110.
DR GeneID; 839890; -.
DR Gramene; AT1G30110.1; AT1G30110.1; AT1G30110.
DR Gramene; AT1G30110.2; AT1G30110.2; AT1G30110.
DR KEGG; ath:AT1G30110; -.
DR Araport; AT1G30110; -.
DR TAIR; locus:2202487; AT1G30110.
DR eggNOG; ENOG502QRQY; Eukaryota.
DR HOGENOM; CLU_087195_3_0_1; -.
DR InParanoid; Q9C6Z2; -.
DR OMA; PLDCVIE; -.
DR OrthoDB; 1602447at2759; -.
DR PhylomeDB; Q9C6Z2; -.
DR BioCyc; ARA:AT1G30110-MON; -.
DR BRENDA; 3.6.1.17; 399.
DR SABIO-RK; Q9C6Z2; -.
DR PRO; PR:Q9C6Z2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6Z2; baseline and differential.
DR Genevisible; Q9C6Z2; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0034432; F:bis(5'-adenosyl)-pentaphosphatase activity; IBA:GO_Central.
DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IDA:TAIR.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015967; P:diadenosine tetraphosphate catabolic process; IDA:TAIR.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IDA:TAIR.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR HAMAP; MF_00298; Nudix_RppH; 1.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR022927; RppH.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..175
FT /note="Nudix hydrolase 25"
FT /id="PRO_0000378337"
FT DOMAIN 7..155
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 40..61
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 40
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q96DE0"
SQ SEQUENCE 175 AA; 19829 MW; 42B6EDE62452530F CRC64;
MENLPPGYRP NVGVCLINSD NLVFVASRLN VPGAWQMPQG GIEDGEDPKS AAMRELQEET
GVVSAEIVSE VPNWLTYDFP PAVKAKVNRL WGGEWHGQAQ KWYLVRLRND EDEKEINLAN
NEADSEFAEW KWAKPEEVVE QAVDYKRPTY EEVIKTFGSF LNDTGRAAKC KSAKW
