IPYR_MYCLE
ID IPYR_MYCLE Reviewed; 162 AA.
AC O69540;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=ML0210;
GN ORFNames=MLCB2548.21;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL023093; CAA18808.1; -; Genomic_DNA.
DR EMBL; AL583917; CAC29718.1; -; Genomic_DNA.
DR PIR; B86935; B86935.
DR RefSeq; NP_301276.1; NC_002677.1.
DR RefSeq; WP_010907600.1; NC_002677.1.
DR PDB; 4ECP; X-ray; 1.80 A; A/B=2-162.
DR PDBsum; 4ECP; -.
DR AlphaFoldDB; O69540; -.
DR SMR; O69540; -.
DR STRING; 272631.ML0210; -.
DR EnsemblBacteria; CAC29718; CAC29718; CAC29718.
DR KEGG; mle:ML0210; -.
DR PATRIC; fig|272631.5.peg.335; -.
DR Leproma; ML0210; -.
DR eggNOG; COG0221; Bacteria.
DR HOGENOM; CLU_073198_1_1_11; -.
DR OMA; DEPTFPG; -.
DR Proteomes; UP000000806; 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;
KW Reference proteome.
FT CHAIN 1..162
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137511"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4ECP"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4ECP"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4ECP"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4ECP"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:4ECP"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:4ECP"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:4ECP"
FT STRAND 71..84
FT /evidence="ECO:0007829|PDB:4ECP"
FT STRAND 87..98
FT /evidence="ECO:0007829|PDB:4ECP"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4ECP"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4ECP"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:4ECP"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:4ECP"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:4ECP"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:4ECP"
SQ SEQUENCE 162 AA; 18533 MW; 5458700F5C26FEC4 CRC64;
MQFDVTIEIP KGQRNKYEVD HKTGRVRLDR YLYTPMAYPT DYGFIEDTLG EDGDPLDALV
LLPEPLFPGV LVEARPVGMF RMVDEHGGDD KVLCVPVNDH RWDHIHGIID VPTFELDAIK
HFFVHYKDLE PGKFVKAADW VGRDEAEAEV QRSVERFKAG GH
