ID GPPA_SHISS Reviewed; 494 AA. AC Q3YVI5; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase; DE EC=3.6.1.40; DE AltName: Full=Guanosine pentaphosphate phosphohydrolase; DE AltName: Full=pppGpp-5'-phosphohydrolase; GN Name=gppA; OrderedLocusNames=SSON_3950; OS Shigella sonnei (strain Ss046). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). CC -!- FUNCTION: Conversion of pppGpp to ppGpp. Guanosine pentaphosphate CC (pppGpp) is a cytoplasmic signaling molecule which together with CC ppGpp controls the "stringent response", an adaptive process that CC allows bacteria to respond to amino acid starvation, resulting in CC the coordinated regulation of numerous cellular activities (By CC similarity). CC -!- CATALYTIC ACTIVITY: Guanosine 5'-triphosphate,3'-diphosphate + CC H(2)O = guanosine 5'-diphosphate,3'-diphosphate + phosphate. CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: CC step 1/2. CC -!- SIMILARITY: Belongs to the gppA/ppx family. GppA subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000038; AAZ90477.1; -; Genomic_DNA. DR RefSeq; YP_312712.1; -. DR GeneID; 3669760; -. DR GenomeReviews; CP000038_GR; SSON_3950. DR KEGG; ssn:SSON_3950; -. DR HOGENOM; Q3YVI5; -. DR OMA; Q3YVI5; QYTDLGW. DR BioCyc; SSON300269:SSO_3950-MON; -. DR GO; GO:0008894; F:guanosine-5'-triphosphate,3'-diphosphate di...; IEA:HAMAP. DR HAMAP; MF_01550; -; 1. DR InterPro; IPR003695; Ppx_GppA. DR Pfam; PF02541; Ppx-GppA; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase. FT CHAIN 1 494 Guanosine-5'-triphosphate,3'-diphosphate FT pyrophosphatase. FT /FTId=PRO_0000194291. SQ SEQUENCE 494 AA; 54871 MW; 423F8AB554A0621E CRC64; MGSTSSLYAA IDLGSNSFHM LVVREVAGSI QTLTRIKRKV RLAAGLNSEN ALSNEAMERG WQCLRLFAER LQDIPPSQIR VVATATLRLA VNAGDFIANA 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 //