ID GPPA_SODGM Reviewed; 499 AA. AC Q2NQB1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 16-JUN-2009, entry version 17. 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=SG2389; OS Sodalis glossinidius (strain morsitans). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Sodalis. OX NCBI_TaxID=343509; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16365377; DOI=10.1101/gr.4106106; RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., RA Hattori M., Aksoy S.; RT "Massive genome erosion and functional adaptations provide insights RT into the symbiotic lifestyle of Sodalis glossinidius in the tsetse RT host."; RL Genome Res. 16:149-156(2006). 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; AP008232; BAE75664.1; -; Genomic_DNA. DR RefSeq; YP_456069.1; -. DR GeneID; 3867360; -. DR GenomeReviews; AP008232_GR; SG2389. DR KEGG; sgl:SG2389; -. DR NMPDR; fig|343509.6.peg.5161; -. DR HOGENOM; Q2NQB1; -. DR OMA; Q2NQB1; QYTDLGW. DR BioCyc; SGLO343509:SG2389-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 1 499 Guanosine-5'-triphosphate,3'-diphosphate FT pyrophosphatase. FT /FTId=PRO_0000314500. SQ SEQUENCE 499 AA; 55655 MW; 01C8F3EABF178AA8 CRC64; MIRATSLYAA IDLGSNSFHM LVVREVAGTL QTLARIKRKV RLAAGLYGDN RLSSDAMQRG WQCLRLFAEH LQDIPPTQVR VVATATLRLA TNAAEFLGPA SAILGCPVQV ISGEEEARLI YQGVAHTTGG SDERLVVDIG GGSTELVVGR GAQALELFSL EMGCVTWLER YFNDRSLTRE NFERAEQAAR EKIRPVAFRL LAQGWQVCVG ASGTVQALQE IMVAQGMDEH ITLSKLLQLK QRAIHCGKLE ELEIEGLTLE RALVFPSGLA ILLAVFAELG ITTMTLAGGA LREGMMYGMM ALPVGGDIRQ RTLENLQRRY QLDTEQAQRV TWLADGFARQ VAEAWQLDER CFTLLRCASM IHEIGLSIDI KRAPQHAAYL VRHTDLPGFT PAQQKLIATL LQNQSNHINL TQLNEQNCLA PRIAQRLCRL MRLAIIFASR RRDDALPAVE LRAAEETLYV ILPQGWLSQH PLRAEYLEQE SQWQSYVHWP LLLEETSQV //