ID W5MN35_LEPOC Unreviewed; 243 AA.
AC W5MN35;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Phospholysine phosphohistidine inorganic pyrophosphate phosphatase {ECO:0000256|ARBA:ARBA00039357};
DE EC=3.6.1.1 {ECO:0000256|ARBA:ARBA00012146};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009794.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000009794.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00037258}.
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 Evidence={ECO:0000256|ARBA:ARBA00000926};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00007958}.
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DR EMBL; AHAT01004034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MN35; -.
DR Ensembl; ENSLOCT00000009805.1; ENSLOCP00000009794.1; ENSLOCG00000008067.1.
DR GeneTree; ENSGT00940000159002; -.
DR HOGENOM; CLU_043473_4_1_1; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000008067; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd07509; HAD_PPase; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01458; HAD-SF-IIA-hyp3; 1.
DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR19288:SF44; PHOSPHOLYSINE PHOSPHOHISTIDINE INORGANIC PYROPHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF13344; Hydrolase_6; 1.
DR Pfam; PF13242; Hydrolase_like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
SQ SEQUENCE 243 AA; 26484 MW; 2F76E3998CF14565 CRC64;
MAEVGWEHCI KDLKGVVLDM CGVLYDSGKG GGVPIPGSIE AVKRIKASDL KLRFCTNETQ
ATRGRFVAKL QKLGFDISVS EVFSPAPAAL SILVQRGLRP HLLVHDDVLP EFDEVDKSNP
NCVVIGDAAD NFSYQNLNDA FRVLIGLEKP ILFSLGRGRY YKETDGLKLD VGVFMKALEY
ACDIEAEVVG KPAKMFFLSA LADMGVEPHE ALMIGDDLVN DVGGAQDCGM KALQVRTGKY
RTE
//
