GPPA_KLEP3
ID GPPA_KLEP3 Reviewed; 499 AA.
AC B5XYZ0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=KPK_5399;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI11046.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XYZ0; -.
DR SMR; B5XYZ0; -.
DR EnsemblBacteria; ACI11046; ACI11046; KPK_5399.
DR KEGG; kpe:KPK_5399; -.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; WQICVGA; -.
DR OrthoDB; 1862004at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000001734; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..499
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_1000192530"
SQ SEQUENCE 499 AA; 55167 MW; A9937C41BDBBF9B8 CRC64;
MSSTSLYAAI DLGSNSFHML VVREVAGSIQ TLSRIKRKVR LAAGLNSDNT LSAEAMERGW
QCLRLFAERL QDIPPTQIRV VATATLRLAV NAEEFLAKAQ EILGTPVQVI SGEEEARLIY
QGVAHTTGGA DQRLVVDIGG ASTELVTGTG AQTTSLFSLS MGCVTWLERY FADRSLTKEN
FDLAEAAARE VLLPIADVLR YHGWKVCVGA SGTVQALQEI MMAQGMDERI TLAKLQQLKQ
RAIQCGRLEE LEIEGLTLER ALVFPSGLAI LIAIFSELNI QCMTLAGGAL REGLVYGMLH
LSVEQDIRSR TLRNIQRRFM IDTEQAQRVA SLASHLLSQL DGSWELDPLS RDLLLSACSL
HEIGLSVDFK RAPQHAAYLV NNLDLPGFTP AQKKLIATLL LNQTNAIDLS SLHQQNAVPP
RVAEHLCRLL RLAILFASRR RDDLLPAIQL AAHDDQLTLT LPENWLAEHP LGREMVDQEC
QWQSYVHWTL RVTSGDTPR