ID   NPP_HORVU               Reviewed;         368 AA.
AC   Q687E1; P83656;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Nucleotide pyrophosphatase/phosphodiesterase;
DE            EC=3.-.-.-;
DE   Flags: Fragments;
GN   Name=npp {ECO:0000312|EMBL:CAE46394.1};
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAE46394.1}
RP   PROTEIN SEQUENCE OF 1-18, NUCLEOTIDE SEQUENCE [MRNA] OF 19-368, FUNCTION,
RP   SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC   STRAIN=cv. Scarlet {ECO:0000269|Ref.1};
RC   TISSUE=Leaf {ECO:0000269|Ref.1, ECO:0000312|EMBL:CAE46394.1};
RA   Nanjo Y., Rodriguez-Lopez M., Munoz F.J., Kurokawa S., Baroja-Fernandez E.,
RA   Mitsui T., Pozueta-Romero J.;
RT   "Cloning, expression and characterization of a glycosylated nucleotide
RT   pyrophosphatase/phosphodiesterase occurring in chloroplasts that belongs to
RT   a widely distributed group of plant nucleotide hydrolases.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes pyrophosphate, phosphodiester and phosphosulfate
CC       linkages of nucleotide-sugars, sulfonucleotides and nucleoside di and
CC       triphosphates. Highest activity observed with the substrates ADP-
CC       glucose and adenosine 5'-phosphosulfate. {ECO:0000269|Ref.1}.
CC   -!- SUBUNIT: Monomer and homomer. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|Ref.1}.
CC   -!- PTM: Glycosylated. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ581660; CAE46394.1; -; mRNA.
DR   AlphaFoldDB; Q687E1; -.
DR   SMR; Q687E1; -.
DR   EnsemblPlants; HORVU.MOREX.r2.4HG0343900.1; HORVU.MOREX.r2.4HG0343900.1; HORVU.MOREX.r2.4HG0343900.
DR   EnsemblPlants; HORVU.MOREX.r2.4HG0343900.1.mrna1; HORVU.MOREX.r2.4HG0343900.1.mrna1; HORVU.MOREX.r2.4HG0343900.1.
DR   EnsemblPlants; HORVU.MOREX.r2.5HG0409490.1; HORVU.MOREX.r2.5HG0409490.1; HORVU.MOREX.r2.5HG0409490.
DR   EnsemblPlants; HORVU.MOREX.r2.5HG0409490.1.mrna1; HORVU.MOREX.r2.5HG0409490.1.mrna1; HORVU.MOREX.r2.5HG0409490.1.
DR   Gramene; HORVU.MOREX.r2.4HG0343900.1; HORVU.MOREX.r2.4HG0343900.1; HORVU.MOREX.r2.4HG0343900.
DR   Gramene; HORVU.MOREX.r2.4HG0343900.1.mrna1; HORVU.MOREX.r2.4HG0343900.1.mrna1; HORVU.MOREX.r2.4HG0343900.1.
DR   Gramene; HORVU.MOREX.r2.5HG0409490.1; HORVU.MOREX.r2.5HG0409490.1; HORVU.MOREX.r2.5HG0409490.
DR   Gramene; HORVU.MOREX.r2.5HG0409490.1.mrna1; HORVU.MOREX.r2.5HG0409490.1.mrna1; HORVU.MOREX.r2.5HG0409490.1.
DR   ExpressionAtlas; Q687E1; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00839; MPP_PAPs; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041792; MPP_PAP.
DR   InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF14008; Metallophos_C; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Glycoprotein; Hydrolase; Plastid.
FT   CHAIN           1..368
FT                   /note="Nucleotide pyrophosphatase/phosphodiesterase"
FT                   /id="PRO_0000057946"
FT   NON_CONS        18..19
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   368 AA;  41746 MW;  47310F115808D288 CRC64;
     AAVRASPDLL GSRGEDTASD GSVVWAKPYT FRAPPTPGQN SLQRIIVFGD MGKAERDGSN
     EFANYQPGSL NTTDRLIEDL DNYDIVFHIG DMPYANGYLS QWDQFTAQVA PISAKKPYMV
     ASGNHERDWP NTGGFFDVKD SGGECGVPAE TMYYYPAENR ANFWYKVDYG MFRFCVGDSE
     HDWREGTPQY KFIEECLSTV DRKHQPWLIF TAHRVLGYSS NSWYADQGSF EEPEGRESLQ
     KLWQRYRVDI AYFGHVHNYE RTCPLYQSQC VNADKTHYSG TMNGTIFVVA GGGGSHLSSY
     TTAIPKWSIF RDHDYGFTKL TAFNHSSLLF EYMKSSDGKV YDSFTIHRDY RDVLSCVHDS
     CFPTTLAS