IPYR_PYRHO
ID IPYR_PYRHO Reviewed; 178 AA.
AC O59570;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=PH1907;
GN ORFNames=PHBT007;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA31032.1; -; Genomic_DNA.
DR PIR; A71205; A71205.
DR RefSeq; WP_010885971.1; NC_000961.1.
DR PDB; 1UDE; X-ray; 2.66 A; A/B/C=1-178.
DR PDBsum; 1UDE; -.
DR AlphaFoldDB; O59570; -.
DR SMR; O59570; -.
DR STRING; 70601.3258349; -.
DR EnsemblBacteria; BAA31032; BAA31032; BAA31032.
DR GeneID; 1442753; -.
DR KEGG; pho:PH1907; -.
DR eggNOG; arCOG01711; Archaea.
DR OMA; DEPTFPG; -.
DR OrthoDB; 103587at2157; -.
DR BRENDA; 3.6.1.1; 5244.
DR EvolutionaryTrace; O59570; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..178
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137557"
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 TURN 11..15
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1UDE"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 85..98
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1UDE"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1UDE"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1UDE"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:1UDE"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1UDE"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1UDE"
FT HELIX 156..170
FT /evidence="ECO:0007829|PDB:1UDE"
SQ SEQUENCE 178 AA; 20834 MW; 138130493C4C890F CRC64;
MNPFHDLEPG PNVPEVVYAL IEIPKGSRNK YELDKETGLL KLDRVLYTPF HYPVDYGIIP
RTWYEDGDPF DIMVIMREPT YPLTIIEARP IGLFKMIDSG DKDYKVLAVP VEDPYFKDWK
DISDVPKAFL DEIAHFFKRY KELEGKEIIV EGWEGAEAAK REILRAIEMY KEKFGKKE
