PPAX_ANOFW
ID PPAX_ANOFW Reviewed; 215 AA.
AC B7GL49;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Pyrophosphatase PpaX {ECO:0000255|HAMAP-Rule:MF_01250};
DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_01250};
GN Name=ppaX {ECO:0000255|HAMAP-Rule:MF_01250}; OrderedLocusNames=Aflv_2539;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
CC -!- FUNCTION: Hydrolyzes pyrophosphate formed during P-Ser-HPr
CC dephosphorylation by HPrK/P. Might play a role in controlling the
CC intracellular pyrophosphate pool. {ECO:0000255|HAMAP-Rule:MF_01250}.
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_01250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01250};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PpaX family.
CC {ECO:0000255|HAMAP-Rule:MF_01250}.
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DR EMBL; CP000922; ACJ34894.1; -; Genomic_DNA.
DR RefSeq; WP_012576033.1; NC_011567.1.
DR AlphaFoldDB; B7GL49; -.
DR SMR; B7GL49; -.
DR STRING; 491915.Aflv_2539; -.
DR PRIDE; B7GL49; -.
DR EnsemblBacteria; ACJ34894; ACJ34894; Aflv_2539.
DR KEGG; afl:Aflv_2539; -.
DR PATRIC; fig|491915.6.peg.2616; -.
DR eggNOG; COG0546; Bacteria.
DR HOGENOM; CLU_045011_19_3_9; -.
DR OMA; LLIFDWD; -.
DR OrthoDB; 1484726at2; -.
DR Proteomes; UP000000742; Chromosome.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01250; Pyrophosphat_PpaX; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR023733; Pyrophosphatase_Ppax.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..215
FT /note="Pyrophosphatase PpaX"
FT /id="PRO_1000139922"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01250"
SQ SEQUENCE 215 AA; 24441 MW; 2441EACB8D5671CD CRC64;
MNINTILFDL DGTLINTNDL IIESFLHTLN HYYPNQYTRE DVLAFIGPPL RDTFEAIDPE
RVDEMIETYR AFNHAHHDAL VKEYETVYDT VQTLHEKGFK LGIVTTKIRH TVNMGLKLTK
LDSFFKCVIT LDDVEHAKPH PEPIEKALAC LQAKPEETLM VGDNHHDILA GKHAGTKTAG
VAWTIKGREH LATYEPDFML EKMSDLLSIL GVTSR