ID M1C958_SOLTU Unreviewed; 400 AA.
AC M1C958;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400062494, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400062494}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400062494};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-
CC nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876,
CC Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029,
CC ChEBI:CHEBI:144051; Evidence={ECO:0000256|ARBA:ARBA00023679};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC Evidence={ECO:0000256|ARBA:ARBA00023679};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC {ECO:0000256|ARBA:ARBA00009595}.
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DR AlphaFoldDB; M1C958; -.
DR STRING; 4113.M1C958; -.
DR PaxDb; 4113-PGSC0003DMT400062490; -.
DR EnsemblPlants; PGSC0003DMT400062490; PGSC0003DMT400062490; PGSC0003DMG400024321.
DR EnsemblPlants; PGSC0003DMT400062492; PGSC0003DMT400062492; PGSC0003DMG400024321.
DR EnsemblPlants; PGSC0003DMT400062493; PGSC0003DMT400062493; PGSC0003DMG400024321.
DR EnsemblPlants; PGSC0003DMT400062494; PGSC0003DMT400062494; PGSC0003DMG400024321.
DR Gramene; PGSC0003DMT400062490; PGSC0003DMT400062490; PGSC0003DMG400024321.
DR Gramene; PGSC0003DMT400062492; PGSC0003DMT400062492; PGSC0003DMG400024321.
DR Gramene; PGSC0003DMT400062493; PGSC0003DMT400062493; PGSC0003DMG400024321.
DR Gramene; PGSC0003DMT400062494; PGSC0003DMT400062494; PGSC0003DMG400024321.
DR Gramene; RHC06H1G2877.2.1; RHC06H1G2877.2.1; RHC06H1G2877.2.
DR eggNOG; KOG3084; Eukaryota.
DR HOGENOM; CLU_037162_0_2_1; -.
DR InParanoid; M1C958; -.
DR OMA; DLVYWAV; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:0019677; P:NAD catabolic process; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006742; P:NADP catabolic process; IBA:GO_Central.
DR CDD; cd03429; NADH_pyrophosphatase; 1.
DR Gene3D; 3.90.79.20; -; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR015375; NADH_PPase-like_N.
DR InterPro; IPR049734; NudC-like_C.
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 PANTHER; PTHR42904:SF6; NAD-CAPPED RNA HYDROLASE NUDT12; 1.
DR PANTHER; PTHR42904; NUDIX HYDROLASE, NUDC SUBFAMILY; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF09296; NUDIX-like; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003476};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115}.
FT DOMAIN 209..339
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 400 AA; 44399 MW; 12F2F0AA1E7A44B0 CRC64;
MSTNFFKSHA FAGNPIKLRT PKPTDPFSPP SALKTLKNLL LGNTHEPHSP NFKILPFRKG
RPLAGSVRDS NEPNWHLGWL SFGDCKAFLE NSEVNLSEDT LVYLGSDSEG DGVYVVYWGI
DVTEAGNGLV KELGGNQFCF VELRTLMVAT DWENASSMGQ LAIAGHARSL LEWHTVSRFC
GFCGGKNILI DAGRRKQCSN ELCKKKIYPR VDPVVIMLVI DKENDRALLS RQSRFVPRMW
SCLAGFMEPG ESLEEAVRRE TWEETGIEVG QVVYHSSQPW PVGPSSMPCQ LMVGFFAYAK
SLDINVDKEE LEDAKWHSRE DVKKALTIAE YKKAQRTAAG KVDQMCKGVE RGQSLSSDFN
VESGELAPMF IPGPFAIANH LISSWVNGVE SQLASSFSNL
//
