GPPA_AERS4
ID GPPA_AERS4 Reviewed; 496 AA.
AC A4STJ8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=ASA_4296;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(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; CP000644; ABO92220.1; -; Genomic_DNA.
DR RefSeq; WP_005320675.1; NC_009348.1.
DR AlphaFoldDB; A4STJ8; -.
DR SMR; A4STJ8; -.
DR STRING; 382245.ASA_4296; -.
DR EnsemblBacteria; ABO92220; ABO92220; ASA_4296.
DR KEGG; asa:ASA_4296; -.
DR PATRIC; fig|382245.13.peg.4261; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; WQICVGA; -.
DR OrthoDB; 1862004at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000000225; 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..496
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_0000314492"
SQ SEQUENCE 496 AA; 55128 MW; DFAEF0947CFD692D CRC64;
MHNSPLYAAI DLGSNSFHML VVREVAGALR TVTKVKRKVR LAAGLDPEFR LSRAAMERGW
DCLRLFSEQL QDIPADNIRV VGTATLRLAT NVDEFLSEAE RVLNHSIEII SGEEEAKTIY
EGVSWTSAGE GNRLVIDIGG ASTELVIGEH SEAKLLNSLH MGCVTWLNNH FGDGELSEAR
FAQAIAAAKA VLEKVAEDYC VLGWRTCVGA SGTVQALQEI MLAQGKSERV TLPKLQELMG
QAIACGRLDR LQLEGLAAER LTVFPSGLAI LIAIFETLNI ESMTLAGGAL REGLIYGLLG
NNHDCDARDR TADSLISCYQ LDKEHAERVR DTAIEAFNQL QPAWRLSKRY GRPILRYAAL
LHEIGLCIEY KKAPQHAAYI IDNIDMPGFT PAQKKLLSAL LFNQRDEFKL ETLEKQGAVT
GRQAIRLARI LRISLILCMR RTQGTVPNFT LQAEEEALTL TLPKGWMDEH YLRASELRLE
VERQQKMGWP TRLLEA