IPYR_THET8
ID IPYR_THET8 Reviewed; 175 AA.
AC P38576; Q5SGW5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
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=TTHA1965;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9644249; DOI=10.1093/oxfordjournals.jbchem.a022100;
RA Satoh T., Samejima T., Watanabe M., Nogi S., Takahashi Y., Kaji H.,
RA Teplyakov A., Obmolova G., Kuranova I., Ishii K.;
RT "Molecular cloning, expression, and site-directed mutagenesis of inorganic
RT pyrophosphatase from Thermus thermophilus HB8.";
RL J. Biochem. 124:79-88(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=7920256; DOI=10.1002/pro.5560030713;
RA Teplyakov A., Obmolova G., Wilson K.S., Ishii K., Kaji H., Samejima T.,
RA Kuranova I.;
RT "Crystal structure of inorganic pyrophosphatase from Thermus
RT thermophilus.";
RL Protein Sci. 3:1098-1107(1994).
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; AB010580; BAA24521.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71788.1; -; Genomic_DNA.
DR RefSeq; WP_011173971.1; NC_006461.1.
DR RefSeq; YP_145231.1; NC_006461.1.
DR PDB; 2PRD; X-ray; 2.00 A; A=2-175.
DR PDBsum; 2PRD; -.
DR AlphaFoldDB; P38576; -.
DR SMR; P38576; -.
DR STRING; 300852.55773347; -.
DR EnsemblBacteria; BAD71788; BAD71788; BAD71788.
DR GeneID; 3169724; -.
DR KEGG; ttj:TTHA1965; -.
DR PATRIC; fig|300852.9.peg.1936; -.
DR eggNOG; COG0221; Bacteria.
DR HOGENOM; CLU_073198_1_2_0; -.
DR OMA; DEPTFPG; -.
DR PhylomeDB; P38576; -.
DR BRENDA; 3.6.1.1; 2305.
DR EvolutionaryTrace; P38576; -.
DR Proteomes; UP000000532; 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 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..175
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137535"
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 140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2PRD"
FT TURN 11..15
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2PRD"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 85..100
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:2PRD"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2PRD"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2PRD"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:2PRD"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:2PRD"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:2PRD"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:2PRD"
SQ SEQUENCE 175 AA; 19216 MW; 01306D30B31DB061 CRC64;
MANLKSLPVG DKAPEVVHMV IEVPRGSGNK YEYDPDLGAI KLDRVLPGAQ FYPGDYGFIP
STLAEDGDPL DGLVLSTYPL LPGVVVEVRV VGLLLMEDEK GGDAKVIGVV AEDQRLDHIQ
DIGDVPEGVK QEIQHFFETY KALEAKKGKW VKVTGWRDRK AALEEVRACI ARYKG
