GPPA_ALIFM
ID GPPA_ALIFM Reviewed; 497 AA.
AC B5FF86;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=VFMJ11_0053;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-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; CP001139; ACH65095.1; -; Genomic_DNA.
DR RefSeq; WP_012532822.1; NC_011184.1.
DR AlphaFoldDB; B5FF86; -.
DR SMR; B5FF86; -.
DR EnsemblBacteria; ACH65095; ACH65095; VFMJ11_0053.
DR KEGG; vfm:VFMJ11_0053; -.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; WQICVGA; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000001857; Chromosome I.
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..497
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_1000192541"
SQ SEQUENCE 497 AA; 55112 MW; 022C81EDB74A0475 CRC64;
MKSSTIPPMY AAIDLGSNSF HMLVVRHING SVQTMAKIKR KVRLAAGLNE NNTLSHEAMQ
RGWDCLSLFA ERLQDIPVEN IRIVGTATLR VASNVDIFLE KANQILGHNI NVIEGEEEAR
MIYQGVAHTS GGNGRRLVVD IGGASTELII GEGFEAQALT SLKMGCVTWL EGYFKDRALT
QKNFDSAIAG AKETLAPILQ QYTDLGWQTC VGASGTVQAL QEIMLAQGMD EVITLAKLKR
LQKQAMQYEH LEELDIDGLT LERALVFPSG LSILIAIFEL LNIDSMTLAG GALREGLCYG
MIDELQHDEV CQRTIKSTQQ RYQLDVEYAQ QVTDLSIQLV QQCGNDWLTE PQALPLLTAA
TQLHEIGMCI DYKKGGEHSA YLINALDLPG FTRAQKHLLG ELLRRYREYF SAMPTQHAVS
DISAQRMLRI LRLAIILTHR RDVNLAPAVT LSEKNDVLSL SIDGTWLAAN PLTRSELEIE
ADKQTNIGWD LVIDARD
