PPAX_ALKHC
ID PPAX_ALKHC Reviewed; 215 AA.
AC Q9K6Y7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=BH3587;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000004; BAB07306.1; -; Genomic_DNA.
DR PIR; C84098; C84098.
DR RefSeq; WP_010899715.1; NC_002570.2.
DR AlphaFoldDB; Q9K6Y7; -.
DR SMR; Q9K6Y7; -.
DR STRING; 272558.10176211; -.
DR EnsemblBacteria; BAB07306; BAB07306; BAB07306.
DR KEGG; bha:BH3587; -.
DR eggNOG; COG0546; Bacteria.
DR HOGENOM; CLU_045011_19_3_9; -.
DR OMA; LLIFDWD; -.
DR OrthoDB; 1484726at2; -.
DR Proteomes; UP000001258; 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; IPR006549; HAD-SF_hydro_IIIA.
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 PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..215
FT /note="Pyrophosphatase PpaX"
FT /id="PRO_0000056837"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01250"
SQ SEQUENCE 215 AA; 24216 MW; EDC7693676BB05B9 CRC64;
MEINTVLFDL DGTLINTNEL IISSFLHTFE TYYPGKYGRK DAIECIGPPL TDSFKRLDPE
RVEEMVATYR KHNHAHHDKL VEPYEGVYET VKTLHEQGFK LAIVTTKIRE TAMKGLKLFG
LDEFFDVIVA LDDVENVKPN PEPLEKAMNA LGAKKEETIM VGDNSHDILG GKNAGVKTAV
VGYAIRGEDY VRQFDPDYVL RSMPDLLDIV GVKAR
