IPYR_CHLTR
ID IPYR_CHLTR Reviewed; 209 AA.
AC O84777;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=CT_772;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(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; AE001273; AAC68367.1; -; Genomic_DNA.
DR PIR; G71473; G71473.
DR RefSeq; NP_220291.1; NC_000117.1.
DR RefSeq; WP_009872152.1; NC_000117.1.
DR PDB; 6WE5; X-ray; 2.25 A; A/B/C=1-209.
DR PDBsum; 6WE5; -.
DR AlphaFoldDB; O84777; -.
DR SMR; O84777; -.
DR STRING; 813.O172_04300; -.
DR EnsemblBacteria; AAC68367; AAC68367; CT_772.
DR GeneID; 884578; -.
DR KEGG; ctr:CT_772; -.
DR PATRIC; fig|272561.5.peg.848; -.
DR HOGENOM; CLU_073198_2_1_0; -.
DR InParanoid; O84777; -.
DR OMA; DEPTFPG; -.
DR Proteomes; UP000000431; 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..209
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137492"
FT BINDING 38
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 64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:6WE5"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6WE5"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 110..129
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:6WE5"
FT TURN 141..145
FT /evidence="ECO:0007829|PDB:6WE5"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6WE5"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:6WE5"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:6WE5"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:6WE5"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:6WE5"
SQ SEQUENCE 209 AA; 23391 MW; 7694093E5ADF0275 CRC64;
MSKTPLSIAH PWHGPVLTRD DYESLCCYIE ITPADSVKFE LDKETGILKV DRPQKFSNFC
PCLYGLLPKT YCGDLSGEYS GQQSNRENIK GDGDPLDICV LTEKNITQGN ILLQARPIGG
IRILDSEEAD DKIIAVLEDD LVYGNIEDIS ECPGTVLDMI QHYFLTYKAT PESLIQAKPA
KIEIVGLYGK KEAQKVIRLA HEDYCNLFM
