IPYR_SYNY3
ID IPYR_SYNY3 Reviewed; 169 AA.
AC P80507; P74337;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 122.
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}; Synonyms=ipyR;
GN OrderedLocusNames=slr1622;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-43, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND FORMYLATION AT MET-1.
RX PubMed=17635582; DOI=10.1111/j.1742-4658.2007.05927.x;
RA Gomez-Garcia M.R., Losada M., Serrano A.;
RT "Comparative biochemical and functional studies of family I soluble
RT inorganic pyrophosphatases from photosynthetic bacteria.";
RL FEBS J. 274:3948-3959(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-20.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
CC -!- FUNCTION: Hydrolyzes PPi generated in anabolic reactions.
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, ECO:0000269|PubMed:17635582};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00209,
CC ECO:0000269|PubMed:17635582};
CC Note=In the presence of Zn(2+) ions, activity is 13% of maximum, in the
CC presence of Mn(2+), Cu(2+), Fe(2+) or Co(2+) ions, activity is very
CC low. In the absence of metal ions, there is no activity.
CC {ECO:0000269|PubMed:17635582};
CC -!- ACTIVITY REGULATION: Inhibited by ATP, but not by fructose 1,6-
CC bisphosphate or 2-phosphoglycerate. {ECO:0000269|PubMed:17635582}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 uM for PPi {ECO:0000269|PubMed:17635582};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00209,
CC ECO:0000269|PubMed:17635582}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00209}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA18431.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ252207; CAC81010.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18431.1; ALT_INIT; Genomic_DNA.
DR PIR; S76172; S76172.
DR AlphaFoldDB; P80507; -.
DR SMR; P80507; -.
DR STRING; 1148.1653518; -.
DR PaxDb; P80507; -.
DR EnsemblBacteria; BAA18431; BAA18431; BAA18431.
DR KEGG; syn:slr1622; -.
DR eggNOG; COG0221; Bacteria.
DR InParanoid; P80507; -.
DR OMA; DEPTFPG; -.
DR PhylomeDB; P80507; -.
DR BRENDA; 3.6.1.1; 382.
DR SABIO-RK; P80507; -.
DR Proteomes; UP000001425; 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 Cytoplasm; Direct protein sequencing; Formylation; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..169
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137534"
FT BINDING 28
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 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 101
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 MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:17635582"
FT CONFLICT 37
FT /note="C -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 19088 MW; 29AED1AABDFBC45D CRC64;
MDLSRIPAQP KAGLINVLIE IPAGSKNKYE FDKDMNCFAL DRVLYSSVQY PYDYGFIPNT
LADDGDPLDG MVIMDQPTFP GCVITARPIG MLEMIDGGDR DEKILCVPAK DPRYTYVKSI
NDLAGHRLDE IAEFFRSYKN LEKKVTEILG WKDVDAVLPL VEECVKNYK
