IPYR_PYRFU
ID IPYR_PYRFU Reviewed; 178 AA.
AC Q8U438;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=PF0257;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL80381.1; -; Genomic_DNA.
DR RefSeq; WP_011011372.1; NZ_CP023154.1.
DR PDB; 1TWL; X-ray; 2.20 A; A=2-178.
DR PDBsum; 1TWL; -.
DR AlphaFoldDB; Q8U438; -.
DR SMR; Q8U438; -.
DR STRING; 186497.PF0257; -.
DR EnsemblBacteria; AAL80381; AAL80381; PF0257.
DR GeneID; 41712047; -.
DR KEGG; pfu:PF0257; -.
DR PATRIC; fig|186497.12.peg.269; -.
DR eggNOG; arCOG01711; Archaea.
DR HOGENOM; CLU_073198_1_2_2; -.
DR OMA; DEPTFPG; -.
DR OrthoDB; 103587at2157; -.
DR PhylomeDB; Q8U438; -.
DR BRENDA; 3.6.1.1; 5243.
DR EvolutionaryTrace; Q8U438; -.
DR Proteomes; UP000001013; 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; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..178
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137556"
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 3..6
FT /evidence="ECO:0007829|PDB:1TWL"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1TWL"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 85..98
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1TWL"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1TWL"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1TWL"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:1TWL"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1TWL"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1TWL"
FT HELIX 156..172
FT /evidence="ECO:0007829|PDB:1TWL"
SQ SEQUENCE 178 AA; 20913 MW; 5879D3422934C9D5 CRC64;
MNPFHDLEPG PDVPEVVYAI IEIPKGSRNK YELDKKTGLL KLDRVLYSPF FYPVDYGIIP
RTWYEDDDPF DIMVIMREPV YPLTIIEARP IGLFKMIDSG DKDYKVLAVP VEDPYFKDWK
DIDDVPKAFL DEIAHFFKRY KELQGKEIIV EGWEGAEAAK REILRAIEMY KEKFGKKE
