GPPA_ECO24
ID GPPA_ECO24 Reviewed; 494 AA.
AC A7ZTY0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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};
GN OrderedLocusNames=EcE24377A_4289;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(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; CP000800; ABV17172.1; -; Genomic_DNA.
DR RefSeq; WP_001299253.1; NC_009801.1.
DR AlphaFoldDB; A7ZTY0; -.
DR SMR; A7ZTY0; -.
DR EnsemblBacteria; ABV17172; ABV17172; EcE24377A_4289.
DR GeneID; 66672318; -.
DR KEGG; ecw:EcE24377A_4289; -.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; WQICVGA; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000001122; 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..494
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_1000068821"
SQ SEQUENCE 494 AA; 54885 MW; 43FDAD909437F5AF CRC64;
MGSTSSLYAA IDLGSNSFHM LVVREVAGSI QTLTRIKRKV RLAAGLNSEN ALSNEAMERG
WQCLRLFAER LQDIPPSQIR VVATATLRLA VNAGDFIAKA QEILGCPVQV ISGEEEARLI
YQGVAHTTGG ADQRLVVDIG GASTELVTGT GAQTTSLFSL SMGCVTWLER YFADRNLGQE
NFDAAEKAAR EVLRPVADEL RYHGWKVCVG ASGTVQALQE IMMAQGMDER ITLEKLQQLK
QRAIHCGRLE ELEIDGLTLE RALVFPSGLA ILIAIFTELN IQCMTLAGGA LREGLVYGML
HLAVEQDIRS RTLRNIQRRF MIDIDQAQRV AKVAANFFDQ VEKEWHLEAI SRDLLISACQ
LHEIGLSVDF KQAPQHAAYL VRNLDLPGFT PAQKKLLATL LLNQTNPVDL SSLHQQNAVP
PRVAEQLCRL LRLAIIFASR RRDDLVPEMT LQANHELLTL TLPQGWLTQH PLGKEIIAQE
SQWQSYVHWP LEVH