NUD26_ARATH
ID NUD26_ARATH Reviewed; 216 AA.
AC Q9CAF2; Q9LPN7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Nudix hydrolase 26, chloroplastic;
DE Short=AtNUDT26;
DE EC=3.6.1.-;
DE AltName: Full=Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical);
DE Flags: Precursor;
GN Name=NUDT26; Synonyms=NUDX26; OrderedLocusNames=At3g10620;
GN ORFNames=F13M14.9, F18K10.24;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 NOMENCLATURE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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).
CC -!- FUNCTION: Mediates the hydrolysis of some nucleoside diphosphate
CC derivatives. Can use diadenosine 5',5'''-P(1)P(5) pentaphosphate
CC (Ap(5)A), diadenosine 5',5'''-P(1)P(4) tetraphosphate (Ap(4)A) and
CC diadenosine 5',5'''-P(1)P(3) triphosphate (Ap(3)A) as substrates.
CC {ECO:0000269|PubMed:18815383}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.6 uM for diadenosine 5',5'''-P(1)P(5) pentaphosphate
CC {ECO:0000269|PubMed:18815383};
CC KM=28.1 uM for diadenosine 5',5'''-P(1)P(4) tetraphosphate
CC {ECO:0000269|PubMed:18815383};
CC Vmax=35.2 umol/min/mg enzyme with diadenosine 5',5'''-P(1)P(5)
CC pentaphosphate as substrate {ECO:0000269|PubMed:18815383};
CC Vmax=50.5 umol/min/mg enzyme with diadenosine 5',5'''-P(1)P(4)
CC tetraphosphate as substrate {ECO:0000269|PubMed:18815383};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18815383}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and
CC inflorescences. {ECO:0000269|PubMed:18815383}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76368.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011560; AAG51386.1; -; Genomic_DNA.
DR EMBL; AC013428; AAF76368.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74935.1; -; Genomic_DNA.
DR EMBL; AF370187; AAK44002.1; -; mRNA.
DR EMBL; AY059145; AAL15251.1; -; mRNA.
DR RefSeq; NP_187673.1; NM_111898.4.
DR AlphaFoldDB; Q9CAF2; -.
DR SMR; Q9CAF2; -.
DR STRING; 3702.AT3G10620.1; -.
DR MetOSite; Q9CAF2; -.
DR PaxDb; Q9CAF2; -.
DR PRIDE; Q9CAF2; -.
DR ProteomicsDB; 248769; -.
DR EnsemblPlants; AT3G10620.1; AT3G10620.1; AT3G10620.
DR GeneID; 820231; -.
DR Gramene; AT3G10620.1; AT3G10620.1; AT3G10620.
DR KEGG; ath:AT3G10620; -.
DR Araport; AT3G10620; -.
DR TAIR; locus:2075840; AT3G10620.
DR eggNOG; ENOG502QSDR; Eukaryota.
DR HOGENOM; CLU_087195_2_0_1; -.
DR InParanoid; Q9CAF2; -.
DR OMA; PCVGIML; -.
DR OrthoDB; 1602447at2759; -.
DR PhylomeDB; Q9CAF2; -.
DR BioCyc; ARA:AT3G10620-MON; -.
DR BRENDA; 3.6.1.B16; 399.
DR SABIO-RK; Q9CAF2; -.
DR PRO; PR:Q9CAF2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9CAF2; baseline and differential.
DR Genevisible; Q9CAF2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0034432; F:bis(5'-adenosyl)-pentaphosphatase 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: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 Chloroplast; Hydrolase; Magnesium; Manganese; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..216
FT /note="Nudix hydrolase 26, chloroplastic"
FT /id="PRO_0000378338"
FT DOMAIN 62..209
FT /note="Nudix hydrolase"
FT MOTIF 95..116
FT /note="Nudix box"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 24617 MW; 8F9446ECFAAB9A5B CRC64;
MALYRPLLLH HPTSPSVTTF LRNYPSKPIK FSSLPFLHRC RKSRVSSSSA RCCSSMESPP
EGYRRNVGVC LMNSSKKIFT ASRLDIPSAW QMPQGGIDEG EDPRVAVMRE LKEETGVHSA
EILAEAPHWI TYDFPPDVRE KLKVRWGSDW KGQAQKWFLL KFTGKDEEIN LLGDGTEKPE
FGEWSWTSPD QVVENAVEFK KPVYKEVMSA FASHLQ
