ID   B9LS63_HALLT            Unreviewed;       177 AA.
AC   B9LS63;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   10-JUN-2026, entry version 80.
DE   RecName: Full=Inorganic pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00209};
DE            EC=3.6.1.1 {ECO:0000256|HAMAP-Rule:MF_00209};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|HAMAP-Rule:MF_00209};
DE            Short=PPase {ECO:0000256|HAMAP-Rule:MF_00209};
GN   Name=ppa {ECO:0000256|HAMAP-Rule:MF_00209};
GN   OrderedLocusNames=Hlac_0304 {ECO:0000313|EMBL:ACM55908.1};
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Halobacteria; Halobacteriales; Haloferacaceae; Halorubrum.
OX   NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM55908.1, ECO:0000313|Proteomes:UP000000740};
RN   [1] {ECO:0000313|EMBL:ACM55908.1, ECO:0000313|Proteomes:UP000000740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC   {ECO:0000313|Proteomes:UP000000740};
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi)
CC       forming two phosphate ions. {ECO:0000256|HAMAP-Rule:MF_00209}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = 2 phosphate + H(+); 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:ARBA00047820, ECO:0000256|HAMAP-
CC         Rule:MF_00209};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00209};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00209}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209}.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00209}.
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DR   EMBL; CP001365; ACM55908.1; -; Genomic_DNA.
DR   RefSeq; WP_012659549.1; NC_012029.1.
DR   AlphaFoldDB; B9LS63; -.
DR   SMR; B9LS63; -.
DR   GeneID; 7401230; -.
DR   KEGG; hla:Hlac_0304; -.
DR   eggNOG; arCOG01711; Archaea.
DR   HOGENOM; CLU_073198_1_2_2; -.
DR   Proteomes; UP000000740; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd00412; pyrophosphatase; 1.
DR   FunFam; 3.90.80.10:FF:000003; Inorganic pyrophosphatase; 1.
DR   Gene3D; 3.90.80.10; Inorganic pyrophosphatase; 1.
DR   HAMAP; MF_00209; Inorganic_PPase; 1.
DR   InterPro; IPR008162; Pyrophosphatase.
DR   InterPro; IPR036649; Pyrophosphatase_sf.
DR   PANTHER; PTHR10286; INORGANIC PYROPHOSPHATASE; 1.
DR   Pfam; PF00719; Pyrophosphatase; 1.
DR   SUPFAM; SSF50324; Inorganic pyrophosphatase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00209};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00209};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00209};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00209}; Reference proteome {ECO:0000313|Proteomes:UP000000740}.
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00209"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00209"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00209"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00209"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00209"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00209"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00209"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00209"
SQ   SEQUENCE   177 AA;  20521 MW;  CDCB5FFFAFAB26FB CRC64;
     MVNLWEDLET GPNAPDEIYA VVECLKGERN KYEYDKDIPS VVLDRVLHSN VHYPYDYGFI
     PQSYYDDEDP FDVMVLVEDQ TFPGCVIEAR PVALMKMDDD GEQDDKVIAV PTEDPRFDHI
     EDLSDLPQQT LDEIDEFFST YKNLEAGKEV ETLGWEDKQA ARDAIEHAQD LYDEEFQ
//