ID GPPA_ERWT9 Reviewed; 494 AA. AC B2VG72; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, 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}; GN OrderedLocusNames=ETA_01930; OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB OS 4357 / Et1/99). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Erwinia. OX NCBI_TaxID=465817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99; RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x; RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., RA Geider K.; RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic RT bacterium in the genus Erwinia."; RL Environ. Microbiol. 10:2211-2222(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}. 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; CU468135; CAO95239.1; -; Genomic_DNA. DR RefSeq; WP_012439959.1; NC_010694.1. DR AlphaFoldDB; B2VG72; -. DR SMR; B2VG72; -. DR STRING; 465817.ETA_01930; -. DR KEGG; eta:ETA_01930; -. DR eggNOG; COG0248; Bacteria. DR HOGENOM; CLU_025908_4_0_6; -. DR OrthoDB; 9793035at2; -. DR UniPathway; UPA00908; UER00885. DR Proteomes; UP000001726; Chromosome. DR GO; GO:0004309; F:exopolyphosphatase activity; IEA:InterPro. 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 Gene3D; 3.30.420.40; -; 1. DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1. DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1. DR HAMAP; MF_01550; GppA; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR022371; Exopolyphosphatase. DR InterPro; IPR023709; Guo-5TP_3DP_PyrP. DR InterPro; IPR048950; Ppx_GppA_C. DR InterPro; IPR003695; Ppx_GppA_N. DR InterPro; IPR030673; PyroPPase_GppA_Ppx. DR NCBIfam; TIGR03706; exo_poly_only; 1. DR PANTHER; PTHR30005; EXOPOLYPHOSPHATASE; 1. DR PANTHER; PTHR30005:SF0; RETROGRADE REGULATION PROTEIN 2; 1. DR Pfam; PF02541; Ppx-GppA; 1. DR Pfam; PF21447; Ppx-GppA_III; 1. DR PIRSF; PIRSF001267; Pyrophosphatase_GppA_Ppx; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1. 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_1000146872" SQ SEQUENCE 494 AA; 54728 MW; 164A4574EE6E56D0 CRC64; MRSASSLYAA IDLGSNSFHM LVVREVAGSI QTIARIKRKV RLAAGLDADN NLSAEAMDRG WQCLRLFSEQ LQDIPPEQIR VVATATLRIA ANAGSFLAQA QKLLGCPVNV ISGEEEARLI YQGVSHTTGG SDKRLVVDIG GGSTELVTGR GSQPTTLYSL SMGCVTWLER YFSDRQLGKV NFEQAEQAAR AMIRPIADSL KAQGWQVCVG ASGTVQALQE IMMAQGMDER ITLNKLQQLK QRAIECGKLE ELEIEGLTLE RALVFPSGLS ILIAIFSELN ISSMTLAGGA LREGLLYGML PLPVDRDIRS RTLHDVQRRF SVDPEQAERV RQLADSFARQ VSLQWKLDDR SRELLGSACL LHEIGLSVDF RQAPQHAAYL VRYLDLPGFT PAQKKLLATL LQNQVGNIDL PLLSQQNALL PRIAERLSRL LRLAIIFASR RRDDRLPAVR LQADDDNLTV TLPSGWLEAH PLRAELLEQE ARWQGYVHWP LIIA //