GPPA_SALAR
ID GPPA_SALAR Reviewed; 494 AA.
AC A9MJ30;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=SARI_03739;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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; CP000880; ABX23539.1; -; Genomic_DNA.
DR RefSeq; WP_000935164.1; NC_010067.1.
DR AlphaFoldDB; A9MJ30; -.
DR SMR; A9MJ30; -.
DR STRING; 41514.SARI_03739; -.
DR EnsemblBacteria; ABX23539; ABX23539; SARI_03739.
DR KEGG; ses:SARI_03739; -.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; WQICVGA; -.
DR OrthoDB; 1862004at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000002084; 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; Reference proteome.
FT CHAIN 1..494
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_1000087731"
SQ SEQUENCE 494 AA; 54910 MW; 413F9A79100FB138 CRC64;
MLNSTSLYAA IDLGSNSFHM LVVREVAGSI QTLTRIKRKV RLAAGLSSDN QLSAEAMERG
WQCLRLFAER LQDIPQPQIR VVATATLRLA VNAGEFIAKA QTILGCPVQV ISGEEEARLI
YQGVAHTTGG AEQRLVVDIG GASTELVTGT GAQTTSLFSL SMGCVTWLEH YFSDRNLAQE
NFDDAEKAAR DVLRPVADKL RFHGWKVCVG ASGTVQALQE IMMAQGMDER ITLAKLQQLK
QRAIQCGRLE ELEIEGLTLE RALVFPSGLA ILIAIFTELN IQFMTLAGGA LREGLVYGML
HLTVDQDICS RTLRNIQRRF IIDTDQANRV AKLAGNFLKQ VENAWHIEPI SRELLLSACQ
LHEIGLSVDF KQAPYHAAYL VRHLDLPGYT PAQKKLLATL LLNQTNPVDL SSLHQQNAVP
PRVAEQLCRL LRLAILFAGR RRDDLVPEIT LQAQNENLTL TLPDGWLAHH PLGKELIDQE
SQWQSYVHWP LDIR