(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BII3_GEOS0

ID   A0A0F6BII3_GEOS0        Unreviewed;       215 AA.
AC   A0A0F6BII3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 22.
DE   RecName: Full=Pyrophosphatase PpaX {ECO:0000256|HAMAP-Rule:MF_01250};
DE            EC=3.6.1.1 {ECO:0000256|HAMAP-Rule:MF_01250};
GN   Name=ppaX {ECO:0000256|HAMAP-Rule:MF_01250};
GN   OrderedLocusNames=GY4MC1_0392 {ECO:0000313|EMBL:ADP73234.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73234.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73234.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73234.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC       Rule:MF_01250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01250};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PpaX
CC       family. {ECO:0000256|HAMAP-Rule:MF_01250}.
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DR   EMBL; CP002293; ADP73234.1; -; Genomic_DNA.
DR   RefSeq; WP_013400002.1; NC_014650.1.
DR   EnsemblBacteria; ADP73234; ADP73234; GY4MC1_0392.
DR   GeneID; 29236950; -.
DR   KEGG; gmc:GY4MC1_0392; -.
DR   KO; K06019; -.
DR   OMA; YLCGKFG; -.
DR   OrthoDB; 1484726at2; -.
DR   BioCyc; GSP581103:G1GOQ-437-MONOMER; -.
DR   Proteomes; UP000002034; 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.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BII3.
DR   SWISS-2DPAGE; A0A0F6BII3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01250,
KW   ECO:0000313|EMBL:ADP73234.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01250}.
FT   ACT_SITE      9      9       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01250}.
SQ   SEQUENCE   215 AA;  24299 MW;  0AD9B3ECE53607EC CRC64;
     MKIRTVLFDL DGTLIDTNEL IIQSFLHTLE KYYPGKYTRE DILPFIGPPL SETFNALDPS
     RAQEMIDTYR AFNHAQHDAL IREFDTVYET IETLHKNGVR LGVVTTKIHQ TAVMGLKKTR
     LEPFFDCVIG LDDVQHAKPD PEPIYKALDL LQSTPDEALM VGDNYHDILA GKNAGTKTAG
     VAWAIKGREY LQQYKPDFML EKMSDLLAIV GVENA
//

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