GPPA_PROMH
ID GPPA_PROMH Reviewed; 502 AA.
AC B4F1V2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, 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=PMI3311;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(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; AM942759; CAR46499.1; -; Genomic_DNA.
DR RefSeq; WP_004246357.1; NC_010554.1.
DR AlphaFoldDB; B4F1V2; -.
DR SMR; B4F1V2; -.
DR STRING; 529507.PMI3311; -.
DR EnsemblBacteria; CAR46499; CAR46499; PMI3311.
DR GeneID; 6800930; -.
DR KEGG; pmr:PMI3311; -.
DR eggNOG; COG0248; Bacteria.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; WQICVGA; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000008319; 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..502
FT /note="Guanosine-5'-triphosphate,3'-diphosphate
FT pyrophosphatase"
FT /id="PRO_1000192531"
SQ SEQUENCE 502 AA; 56417 MW; 4FFBECABE8723947 CRC64;
MLKSSSLYAA IDLGSNSFHM LVVREIAGSI QVLSRVKRKV RLAAGLNKEN ELSEQAMERG
WQCLRLFSEY LRDIPAEQIR VVATATLRIA KNADIFVAKA SEILGNTVHV ISGEEEARLI
YRGVAHTTGG AEQRLVVDIG GGSTELVTGT GAKTTQLMSL SMGCVTWLER YFSDRSLTEE
NFAQAQQAAK AILAPVAEKL IQQGWQVCVG ASGTVQALQE IMIAQGMDEL ITLPKLERLK
QKAIECGKLE ELEIEGLTFE RALVFPSGLA ILIAIFETLH IENMILAGGA LREGLVYGML
HLPIEQDIRQ RTLRNIQRRF QIDIEQAHRV QQLAEHFFIQ VSKSWQLDNR CRELLSSACA
LHEIGLSVDF RQAPSHASYL VSHLDLPGYT PAQRRLIASF LRNQKGIIDL APLNQQNALP
INQAYRLVRL LRLAIIFASR RRDDTLPALR LRTEDEKLII TLPHQWIAEH PLRAENLHEE
IQLQSYVHWP LMLEEQNNSR IG