GPPA_YERPY
ID GPPA_YERPY Reviewed; 498 AA.
AC B1JQ12;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01550};
DE EC=3.6.1.40 {ECO:0000255|HAMAP-Rule:MF_01550};
DE AltName: Full=Guanosine pentaphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01550};
DE AltName: Full=pppGpp-5'-phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_01550};
GN Name=gppA {ECO:0000255|HAMAP-Rule:MF_01550}; OrderedLocusNames=YPK_4037;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of pppGpp to ppGpp. Guanosine
CC pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which
CC together with ppGpp controls the 'stringent response', an adaptive
CC process that allows bacteria to respond to amino acid starvation,
CC resulting in the coordinated regulation of numerous cellular
CC activities. {ECO:0000255|HAMAP-Rule:MF_01550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine 3'-diphosphate 5'-triphosphate + H2O = guanosine
CC 3',5'-bis(diphosphate) + H(+) + phosphate; Xref=Rhea:RHEA:13073,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:77828, ChEBI:CHEBI:142410; EC=3.6.1.40;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01550};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_01550}.
CC -!- SIMILARITY: Belongs to the GppA/Ppx family. GppA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01550}.
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DR EMBL; CP000950; ACA70299.1; -; Genomic_DNA.
DR RefSeq; WP_002230566.1; NC_010465.1.
DR AlphaFoldDB; B1JQ12; -.
DR SMR; B1JQ12; -.
DR EnsemblBacteria; ACA70299; ACA70299; YPK_4037.
DR KEGG; ypy:YPK_4037; -.
DR OMA; WQICVGA; -.
DR UniPathway; UPA00908; UER00885.
DR GO; GO:0004309; F:exopolyphosphatase activity; IEA:InterPro.
DR GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015974; P:guanosine pentaphosphate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01550; GppA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR022371; Exopolyphosphatase.
DR InterPro; IPR023709; Guo-5TP_3DP_PyrP.
DR InterPro; IPR003695; Ppx_GppA.
DR InterPro; IPR030673; PyroPPase_GppA_Ppx.
DR Pfam; PF02541; Ppx-GppA; 1.
DR PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR03706; exo_poly_only; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..498
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_1000192544"
SQ SEQUENCE 498 AA; 55926 MW; 583A72F958AFFEB5 CRC64;
MMLSSTSLYA AIDLGSNSFH MLVVREVAGS IQTLARIKRK VRLAAGLDNQ NHLSQEAMER
GWQCLKLFSE RLQDIPLDQI RVVATATLRL ASNADEFLRT ATEILGCPIQ VISGEEEARL
IYHGVAHTTG GPEQRLVVDI GGGSTELVTG NGAQANILVS LSMGCVTWLE RYFGDRHLAK
ENFERAELAA HEMIKPVAQR FREHGWQVCV GASGTVQALQ EIMVAQGMDE LITLAKLQQL
KQRAIQCGKL EELEIPGLTL ERALVFPSGL SILIAIFQEL SIESMTLAGG ALREGLVYGM
LHLPVEQDIR RRTLRNLQRR YLLDTEQAKR VSCLADNFFL QVEKEWHLDG RCREFLQNAC
LIHEIGLSVD FKHAPQHAAY LIRNLDLPGF TPAQKLLLSA LLQNQSDTID LSLLNQQNAL
PADMAQHLCR LLRLAIIFSS RRRDDTLPAV RLRADNNALY VLVPQGWLEQ HPYRAEALEQ
ESHWQSYVQW PLLLEELS