IPYR_SULTO
ID IPYR_SULTO Reviewed; 172 AA.
AC Q974Y8;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 107.
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=STK_05240;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-21; 46-65 AND
RP 112-123.
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=9972267; DOI=10.1271/bbb.62.2408;
RA Wakagi T., Oshima T., Imamura H., Matsuzawa H.;
RT "Cloning of the gene for inorganic pyrophosphatase from a thermoacidophilic
RT archaeon, Sulfolobus sp. strain 7, and overproduction of the enzyme by
RT coexpression of tRNA for arginine rare codon.";
RL Biosci. Biotechnol. Biochem. 62:2408-2414(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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 -!- MISCELLANEOUS: Maximal activity at 95 Celsius degrees.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00209}.
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DR EMBL; BA000023; BAB65519.2; -; Genomic_DNA.
DR PIR; JE0392; JE0392.
DR RefSeq; WP_052846890.1; NC_003106.2.
DR AlphaFoldDB; Q974Y8; -.
DR SMR; Q974Y8; -.
DR STRING; 273063.STK_05240; -.
DR EnsemblBacteria; BAB65519; BAB65519; STK_05240.
DR GeneID; 1458469; -.
DR KEGG; sto:STK_05240; -.
DR PATRIC; fig|273063.9.peg.602; -.
DR eggNOG; arCOG01711; Archaea.
DR OMA; DEPTFPG; -.
DR OrthoDB; 103587at2157; -.
DR Proteomes; UP000001015; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..172
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137561"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
SQ SEQUENCE 172 AA; 19435 MW; 87F5C8F98A0343DA CRC64;
MKLSPGKKAP DEVNVLIEIP LGSNIKYEYD EEEEVVKVDR ILYTSMVYPF NYGFIPGTLE
EDGDPLDVLV ISNYPLLPGT AIEVRPIGIL YMRDEEGEDA KIIAVPKDKV DPTFSNIKDI
IDLPQAIKDK INHFFEHYKE LEPGKWVKIS GWGGVSEAKT RINEAIKRAN SK
