ID   LHPP_XENLA              Reviewed;         270 AA.
AC   Q3B8E3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase;
DE            EC=3.1.3.-;
DE            EC=3.6.1.1;
GN   Name=lhpp;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3-
CC       phosphohistidine and 6-phospholysine. Has broad substrate specificity
CC       and can also hydrolyze inorganic diphosphate, but with lower efficiency
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474; EC=3.6.1.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC106524; AAI06525.1; -; mRNA.
DR   RefSeq; NP_001089769.1; NM_001096300.1.
DR   AlphaFoldDB; Q3B8E3; -.
DR   SMR; Q3B8E3; -.
DR   DNASU; 734833; -.
DR   GeneID; 734833; -.
DR   KEGG; xla:734833; -.
DR   CTD; 734833; -.
DR   Xenbase; XB-GENE-955679; lhpp.S.
DR   OrthoDB; 982374at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 734833; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; ISS:UniProtKB.
DR   CDD; cd07509; HAD_PPase; 1.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006355; LHPP/HDHD2.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01458; HAD-SF-IIA-hyp3; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..270
FT                   /note="Phospholysine phosphohistidine inorganic
FT                   pyrophosphate phosphatase"
FT                   /id="PRO_0000305078"
FT   BINDING         14..16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         52..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  29215 MW;  D26483F92FDD74B8 CRC64;
     MAAWANGVRA VLLDVSGVLY DSGGAGGGSA IQGSVDAVNR IRHAGLKLRF CTNESQATRS
     HFAQKLKRFG FSISEEEVTA PGPAATRLMK ERGLRPHLLV HNDLLPEFES VEKSDPNCVL
     IGDAAENFSY KNVNRAFQVL INLQKPVLIS LGKGRYYKET DGLKLDVGAY MKALEYACDI
     KAEVVGKPSP NFFLSALEEM GAKPEEALMI GDDIVHDIGG AKSCGLRAVL VRTGKYRPSD
     EKHPEVTADG YVNNLAHAVD ILLASQDCNQ