IPYR_PSEAE
ID IPYR_PSEAE Reviewed; 175 AA.
AC Q9HWZ6;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=PA4031;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG07418.1; -; Genomic_DNA.
DR PIR; C83141; C83141.
DR RefSeq; NP_252720.1; NC_002516.2.
DR RefSeq; WP_003093248.1; NZ_QZGE01000013.1.
DR PDB; 4XEL; X-ray; 2.00 A; A/B=1-175.
DR PDBsum; 4XEL; -.
DR AlphaFoldDB; Q9HWZ6; -.
DR SMR; Q9HWZ6; -.
DR STRING; 287.DR97_3836; -.
DR PaxDb; Q9HWZ6; -.
DR PRIDE; Q9HWZ6; -.
DR EnsemblBacteria; AAG07418; AAG07418; PA4031.
DR GeneID; 879025; -.
DR KEGG; pae:PA4031; -.
DR PATRIC; fig|208964.12.peg.4222; -.
DR PseudoCAP; PA4031; -.
DR HOGENOM; CLU_073198_1_0_6; -.
DR InParanoid; Q9HWZ6; -.
DR OMA; DEPTFPG; -.
DR PhylomeDB; Q9HWZ6; -.
DR BioCyc; PAER208964:G1FZ6-4104-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:PseudoCAP.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
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..175
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137517"
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 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:4XEL"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:4XEL"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4XEL"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4XEL"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4XEL"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4XEL"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4XEL"
FT STRAND 85..98
FT /evidence="ECO:0007829|PDB:4XEL"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4XEL"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:4XEL"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:4XEL"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4XEL"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:4XEL"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:4XEL"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:4XEL"
SQ SEQUENCE 175 AA; 19396 MW; D900807026F4996C CRC64;
MSYSKIPAGK DLPNDIYVAI EIPANHAPIK YEIDKDTDCL FVDRFMATPM FYPANYGFIP
NTLADDGDPL DVLVVTPYPV APGSVIRARP VGVLHMTDEA GGDAKLIAVP HDKLSVLYKD
VKEYTDLPAL LLEQIKHFFE NYKDLEKGKW VKVEGWGNAD AARAEITKAV AAFQK
