ID   LHPP_BOVIN              Reviewed;         270 AA.
AC   Q0VD18;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase;
DE            EC=3.1.3.-;
DE            EC=3.6.1.1;
GN   Name=LHPP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND TISSUE SPECIFICITY.
RX   PubMed=9448729; DOI=10.1006/abbi.1997.0480;
RA   Hiraishi H., Yokoi F., Kumon A.;
RT   "3-phosphohistidine and 6-phospholysine are substrates of a 56-kDa
RT   inorganic pyrophosphatase from bovine liver.";
RL   Arch. Biochem. Biophys. 349:381-387(1998).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX   PubMed=12801912; DOI=10.1093/jb/mvg078;
RA   Yokoi F., Hiraishi H., Izuhara K.;
RT   "Molecular cloning of a cDNA for the human phospholysine phosphohistidine
RT   inorganic pyrophosphate phosphatase.";
RL   J. Biochem. 133:607-614(2003).
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
CC       efficiency. {ECO:0000269|PubMed:9448729}.
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; Evidence={ECO:0000269|PubMed:9448729};
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12801912,
CC       ECO:0000269|PubMed:9448729}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC       {ECO:0000269|PubMed:9448729}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC119882; AAI19883.1; -; mRNA.
DR   RefSeq; NP_001074381.1; NM_001080912.1.
DR   AlphaFoldDB; Q0VD18; -.
DR   SMR; Q0VD18; -.
DR   STRING; 9913.ENSBTAP00000047621; -.
DR   PaxDb; Q0VD18; -.
DR   PRIDE; Q0VD18; -.
DR   Ensembl; ENSBTAT00000056613; ENSBTAP00000047621; ENSBTAG00000010957.
DR   GeneID; 534183; -.
DR   KEGG; bta:534183; -.
DR   CTD; 64077; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010957; -.
DR   VGNC; VGNC:30870; LHPP.
DR   eggNOG; KOG3040; Eukaryota.
DR   GeneTree; ENSGT00940000159002; -.
DR   HOGENOM; CLU_043473_4_1_1; -.
DR   InParanoid; Q0VD18; -.
DR   OMA; GPCIDVG; -.
DR   OrthoDB; 982374at2759; -.
DR   TreeFam; TF314344; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000010957; Expressed in laryngeal cartilage and 103 other tissues.
DR   ExpressionAtlas; Q0VD18; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
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; 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; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01458; HAD-SF-IIA-hyp3; 1.
PE   1: Evidence at protein 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_0000305073"
FT   BINDING         17..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         54..55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  29180 MW;  9CAC9DB3EADA8E26 CRC64;
     MAAWGERLAG VRGVLLDISG VLYDGGEGGG AAIAGSVEAV ARLKRSRLKV RFCTNESQKS
     RADLVGLLRR LGFDVSEGEV TAPAPAACLI LKQRGLRPHL LVHDGVRSEF DQIDTSNPNC
     VVIADAGEGF SYQNMNKAFQ VLMELENPVL FSLGKGRYYK ETSGLMLDVG PYMKALEYAC
     GIEAEVVGKP SPEFFKSALQ EMGVEAHEAI MIGDDIVGDV GGAQRYGMRA LQVRTGKFRP
     SDEHHPEVKA DGYVDNLAEA VDLLLQHADK