ID   IPYR_DESVH              Reviewed;          29 AA.
AC   P19371;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Inorganic pyrophosphatase;
DE            EC=3.6.1.1;
DE   AltName: Full=Pyrophosphate phospho-hydrolase;
DE            Short=PPase;
DE   Flags: Fragment;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2168174; DOI=10.1016/0006-291x(90)91394-8;
RA   Liu M.-Y., le Gall J.;
RT   "Purification and characterization of two proteins with inorganic
RT   pyrophosphatase activity from Desulfovibrio vulgaris: rubrerythrin and a
RT   new, highly active, enzyme.";
RL   Biochem. Biophys. Res. Commun. 171:313-318(1990).
CC   -!- FUNCTION: Inorganic pyrophosphatase is an essential enzyme for the
CC       activation of sulfate by sulfate reducing bacteria. This is a high
CC       activity pyrophosphatase.
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;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
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DR   PIR; A35687; A35687.
DR   AlphaFoldDB; P19371; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Periplasm.
FT   CHAIN           1..>29
FT                   /note="Inorganic pyrophosphatase"
FT                   /id="PRO_0000137565"
FT   NON_TER         29
SQ   SEQUENCE   29 AA;  3201 MW;  3FC5792360F2227B CRC64;
     NYTIGNDNVL TEPLSEIKTA GLMYKMGVQ