GPPA_SHIFL
ID GPPA_SHIFL Reviewed; 494 AA.
AC Q83PI3; Q7UB36;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 4.
DT 25-MAY-2022, entry version 103.
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=SF3852, S3907;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN45289.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18908.1; -; Genomic_DNA.
DR RefSeq; NP_709582.2; NC_004337.2.
DR RefSeq; WP_000535982.1; NZ_WPGW01000028.1.
DR AlphaFoldDB; Q83PI3; -.
DR SMR; Q83PI3; -.
DR STRING; 198214.SF3852; -.
DR EnsemblBacteria; AAN45289; AAN45289; SF3852.
DR EnsemblBacteria; AAP18908; AAP18908; S3907.
DR GeneID; 1026029; -.
DR GeneID; 58389378; -.
DR KEGG; sfl:SF3852; -.
DR KEGG; sfx:S3907; -.
DR PATRIC; fig|198214.7.peg.4543; -.
DR HOGENOM; CLU_025908_4_0_6; -.
DR OMA; WQICVGA; -.
DR OrthoDB; 1862004at2; -.
DR UniPathway; UPA00908; UER00885.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000194290"
SQ SEQUENCE 494 AA; 54942 MW; 826EF855C75819AF CRC64;
MGSTSSLYAA IDLGSNSFHM LVVREVAGSI QTLTRIKRKV RLAAGLNSEN DLSNEAMERG
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 VENEWHLEAI SRDLLISACQ
LHEIGLSVDF KQAPQHAAYL VRNLDLPGFT PAQKKLLATL LLNQTNPVDL SSLHQQNAVP
PRVAEQLCRL LRLAIIFASR RRDDLVPEMT LQANHELLTL TLPQGWLTQH PLGKEIIAQE
NQWQSYVHWP LEVH
