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IPYR_RHILO
ID   IPYR_RHILO              Reviewed;         177 AA.
AC   Q98ER2;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00209};
DE            EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00209};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00209};
DE            Short=PPase {ECO:0000255|HAMAP-Rule:MF_00209};
GN   Name=ppa {ECO:0000255|HAMAP-Rule:MF_00209}; OrderedLocusNames=mll4120;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi)
CC       forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.
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:0000255|HAMAP-
CC         Rule:MF_00209};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00209};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00209}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00209}.
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DR   EMBL; BA000012; BAB50855.1; -; Genomic_DNA.
DR   RefSeq; WP_010912198.1; NC_002678.2.
DR   AlphaFoldDB; Q98ER2; -.
DR   SMR; Q98ER2; -.
DR   STRING; 266835.14024251; -.
DR   EnsemblBacteria; BAB50855; BAB50855; BAB50855.
DR   GeneID; 66681386; -.
DR   KEGG; mlo:mll4120; -.
DR   eggNOG; COG0221; Bacteria.
DR   HOGENOM; CLU_073198_1_0_5; -.
DR   OMA; DEPTFPG; -.
DR   OrthoDB; 1767807at2; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphatase 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   Gene3D; 3.90.80.10; -; 1.
DR   HAMAP; MF_00209; Inorganic_PPase; 1.
DR   InterPro; IPR008162; Pyrophosphatase.
DR   InterPro; IPR036649; Pyrophosphatase_sf.
DR   PANTHER; PTHR10286; PTHR10286; 1.
DR   Pfam; PF00719; Pyrophosphatase; 1.
DR   SUPFAM; SSF50324; SSF50324; 1.
DR   PROSITE; PS00387; PPASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..177
FT                   /note="Inorganic pyrophosphatase"
FT                   /id="PRO_0000137524"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         66
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
SQ   SEQUENCE   177 AA;  19971 MW;  E99FA9C967457F15 CRC64;
     MRIEAIATGK NPPEDVNVII EVPIGGEPIK YEMDKEAGTL FVDRFLHTSM RYPGNYGFVP
     HTLSGDGDPI DVLVCNTRAL VPGCVINVRP IGVLVMEDNA GQDEKVIAVP SPKLTLRYEN
     VTEYTHLPEI TRQQVQHFFE HYKDLEPGKW VKIEGWHDSK YAKKMIVDAI ERAKKGK
 
 
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