NUD27_ARATH
ID NUD27_ARATH Reviewed; 227 AA.
AC Q9FNH4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Nudix hydrolase 27, chloroplastic;
DE Short=AtNUDT27;
DE EC=3.6.1.-;
DE Flags: Precursor;
GN Name=NUDT27; Synonyms=NUDX27; OrderedLocusNames=At5g06340;
GN ORFNames=MHF15.14;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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) as substrates. {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=87.4 uM for diadenosine 5',5'''-P(1)P(5) pentaphosphate
CC {ECO:0000269|PubMed:18815383};
CC Vmax=0.15 umol/min/mg enzyme with diadenosine 5',5'''-P(1)P(5)
CC pentaphosphate 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}.
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DR EMBL; AF372941; AAK50081.1; -; mRNA.
DR EMBL; AY113163; AAM47466.1; -; mRNA.
DR EMBL; AB006700; BAB08956.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91004.1; -; Genomic_DNA.
DR RefSeq; NP_196252.1; NM_120717.5.
DR AlphaFoldDB; Q9FNH4; -.
DR SMR; Q9FNH4; -.
DR BioGRID; 15801; 1.
DR IntAct; Q9FNH4; 1.
DR STRING; 3702.AT5G06340.1; -.
DR PaxDb; Q9FNH4; -.
DR PRIDE; Q9FNH4; -.
DR ProteomicsDB; 248850; -.
DR EnsemblPlants; AT5G06340.1; AT5G06340.1; AT5G06340.
DR GeneID; 830522; -.
DR Gramene; AT5G06340.1; AT5G06340.1; AT5G06340.
DR KEGG; ath:AT5G06340; -.
DR Araport; AT5G06340; -.
DR TAIR; locus:2164220; AT5G06340.
DR eggNOG; ENOG502SKZJ; Eukaryota.
DR HOGENOM; CLU_087195_2_0_1; -.
DR InParanoid; Q9FNH4; -.
DR OMA; IAEIPNW; -.
DR OrthoDB; 1602447at2759; -.
DR PhylomeDB; Q9FNH4; -.
DR BioCyc; ARA:AT5G06340-MON; -.
DR SABIO-RK; Q9FNH4; -.
DR PRO; PR:Q9FNH4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNH4; baseline and differential.
DR Genevisible; Q9FNH4; 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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
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..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..227
FT /note="Nudix hydrolase 27, chloroplastic"
FT /id="PRO_0000378339"
FT DOMAIN 61..208
FT /note="Nudix hydrolase"
FT MOTIF 94..115
FT /note="Nudix box"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 25864 MW; F8E6CE397815F2E0 CRC64;
MAVKASGFIG KSAISVHLDF SSFPVKFSCL KQFSVSSPKP LVVLSVALSS PARTVESPPV
GYRKNVGICL VSPCRKIFTA SKIHIPDTWQ MPQGGADEGE DLRNAAFREL REETGVTSAE
FIAEIPNWLT YDFPREVKDK LNRKWRTSYK GQAQKWFLFK FTGKEEEINL LGDGTAKPEF
KVWSWMLPEQ VIEHAVYFKR PVYEHVIKQF NPYFVDEEKD SMNSSKD
