IPYR_NEIMB
ID IPYR_NEIMB Reviewed; 177 AA.
AC Q9K0G4;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=NMB0641;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(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; AE002098; AAF41064.1; -; Genomic_DNA.
DR PIR; F81175; F81175.
DR RefSeq; NP_273684.1; NC_003112.2.
DR RefSeq; WP_002219633.1; NC_003112.2.
DR PDB; 5TEA; X-ray; 1.85 A; A/B/C/D/E/F=1-177.
DR PDBsum; 5TEA; -.
DR AlphaFoldDB; Q9K0G4; -.
DR SMR; Q9K0G4; -.
DR STRING; 122586.NMB0641; -.
DR PaxDb; Q9K0G4; -.
DR EnsemblBacteria; AAF41064; AAF41064; NMB0641.
DR GeneID; 61280871; -.
DR KEGG; nme:NMB0641; -.
DR PATRIC; fig|122586.8.peg.810; -.
DR HOGENOM; CLU_073198_1_2_4; -.
DR OMA; DEPTFPG; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..177
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137515"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 57
FT /ligand="substrate"
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 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 104
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 5..7
FT /evidence="ECO:0007829|PDB:5TEA"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:5TEA"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:5TEA"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5TEA"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:5TEA"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:5TEA"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5TEA"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5TEA"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:5TEA"
FT STRAND 86..99
FT /evidence="ECO:0007829|PDB:5TEA"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:5TEA"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:5TEA"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5TEA"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:5TEA"
FT TURN 142..146
FT /evidence="ECO:0007829|PDB:5TEA"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:5TEA"
FT HELIX 159..175
FT /evidence="ECO:0007829|PDB:5TEA"
SQ SEQUENCE 177 AA; 19811 MW; 6017182C446A8567 CRC64;
MADFNQILTP GDVDGGIINV VNEIPAGSNH KIEWNRKLAA FQLDRVEPAI FAKPTNYGFI
PQTLDEDGDE LDVLLVTEQP LATGVFLEAR VIGVMKFVDD GEVDDKIVCV PADDRNNGNA
YKTLSDLPQQ LIKQIEFHFN HYKDLKKAGT TKVESWGDAE EAKKVIKESI ERWNKQA
