IPYR_SULAC
ID IPYR_SULAC Reviewed; 173 AA.
AC P50308; Q4JA63;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=Saci_0955;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=7771779; DOI=10.1006/abbi.1995.1277;
RA Meyer W., Moll R., Kath T., Schaefer G.;
RT "Purification, cloning, and sequencing of archaebacterial pyrophosphatase
RT from the extreme thermoacidophile Sulfolobus acidocaldarius.";
RL Arch. Biochem. Biophys. 319:149-156(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=10386872; DOI=10.1110/ps.8.6.1218;
RA Leppaenen V.-M., Nummelin H., Hansen T., Lahti R., Schaefer G., Goldman A.;
RT "Sulfolobus acidocaldarius inorganic pyrophosphatase: structure,
RT thermostability, and effect of metal ion in an archael pyrophosphatase.";
RL Protein Sci. 8:1218-1231(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; X81842; CAA57434.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80317.1; -; Genomic_DNA.
DR PIR; S65965; S57617.
DR RefSeq; WP_011277819.1; NC_007181.1.
DR PDB; 1QEZ; X-ray; 2.70 A; A/B/C/D/E/F=1-173.
DR PDBsum; 1QEZ; -.
DR AlphaFoldDB; P50308; -.
DR SMR; P50308; -.
DR STRING; 330779.Saci_0955; -.
DR PRIDE; P50308; -.
DR EnsemblBacteria; AAY80317; AAY80317; Saci_0955.
DR GeneID; 3472897; -.
DR KEGG; sai:Saci_0955; -.
DR PATRIC; fig|330779.12.peg.916; -.
DR eggNOG; arCOG01711; Archaea.
DR HOGENOM; CLU_073198_1_0_2; -.
DR OMA; DEPTFPG; -.
DR BRENDA; 3.6.1.1; 6160.
DR EvolutionaryTrace; P50308; -.
DR Proteomes; UP000001018; 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 CHAIN 1..173
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137559"
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"
FT TURN 7..11
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1QEZ"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 81..94
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:1QEZ"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1QEZ"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1QEZ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1QEZ"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:1QEZ"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:1QEZ"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1QEZ"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:1QEZ"
SQ SEQUENCE 173 AA; 19381 MW; 15FF27EED2B79D72 CRC64;
MKLSPGKNAP DVVNVLVEIP QGSNIKYEYD DEEGVIKVDR VLYTSMNYPF NYGFIPGTLE
EDGDPLDVLV ITNYQLYPGS VIEVRPIGIL YMKDEEGEDA KIVAVPKDKT DPSFSNIKDI
NDLPQATKNK IVHFFEHYKE LEPGKYVKIS GWGSATEAKN RIQLAIKRVS GGQ
