ID   GPPA_PHOPR              Reviewed;         497 AA.
AC   Q6LLL4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=PBPRA3543;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378674; CAG21814.1; -; Genomic_DNA.
DR   RefSeq; WP_011220054.1; NC_006370.1.
DR   AlphaFoldDB; Q6LLL4; -.
DR   SMR; Q6LLL4; -.
DR   STRING; 298386.PBPRA3543; -.
DR   EnsemblBacteria; CAG21814; CAG21814; PBPRA3543.
DR   KEGG; ppr:PBPRA3543; -.
DR   eggNOG; COG0248; Bacteria.
DR   HOGENOM; CLU_025908_4_0_6; -.
DR   OMA; WQICVGA; -.
DR   OrthoDB; 1862004at2; -.
DR   UniPathway; UPA00908; UER00885.
DR   Proteomes; UP000000593; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Guanosine-5'-triphosphate,3'-diphosphate
FT                   pyrophosphatase"
FT                   /id="PRO_0000194283"
SQ   SEQUENCE   497 AA;  55419 MW;  B19477BE5ECF3E99 CRC64;
     MERNPISPLY AAIDLGSNSF HMWIVREVAG SVQTLAKIKR KVRLAAGLNS QNELSEEAMQ
     RGWDCLSLFA ERLQDIPAER VRIIGTAALR TAVNADIFLS KAKDILGSKV DVIPGEEEAR
     IIYQGVAHTS GGSDKRLVVD IGGASTEVII GEGFDASALT SLKIGCVTWL ERYFKDRYLT
     AENFDAAIDA AKNAIEPIVE QYTQLGWETC VGASGTVQAL QEIMLAQGMD EIITLSKLKR
     MQRQAMQYER LEDLDIEGLT LERALVFPSG LSILIAVFES LNIESMTLAG GALREGMVYE
     MMSKMRHHDV RERTLTSVQE RFQLDTSHAS AVTNTAMALL SRCDEEWQLE PQAQYLLHAS
     VCLHEIGTSI EFKKSGEHAA YLINHIDLPG FTRAQKHLIA ELLRRFREQL TSLPEQHALS
     AQNAARILRL LRLAVILCHR RDHNQQPPFS LSVAENKLVL TLPAAWLLAN PLSHVELQQE
     ATRQTDMGWP LVLEESE