(data stored in ACNUC7421 zone)

SWISSPROT: GPPA_AERHH

ID   GPPA_AERHH              Reviewed;         496 AA.
AC   A0KEG8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 69.
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=AHA_0096;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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 =
CC         guanosine 3',5'-bis(diphosphate) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:13073, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:77828, ChEBI:CHEBI:142410;
CC         EC=3.6.1.40; Evidence={ECO:0000255|HAMAP-Rule:MF_01550};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP:
CC       step 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}.
DR   EMBL; CP000462; ABK39541.1; -; Genomic_DNA.
DR   RefSeq; WP_011704128.1; NC_008570.1.
DR   RefSeq; YP_854621.1; NC_008570.1.
DR   SMR; A0KEG8; -.
DR   STRING; 380703.AHA_0096; -.
DR   EnsemblBacteria; ABK39541; ABK39541; AHA_0096.
DR   GeneID; 4490991; -.
DR   KEGG; aha:AHA_0096; -.
DR   PATRIC; fig|380703.7.peg.88; -.
DR   eggNOG; ENOG4105C9X; Bacteria.
DR   eggNOG; COG0248; LUCA.
DR   HOGENOM; HOG000258672; -.
DR   KO; K01524; -.
DR   OMA; WQICVGA; -.
DR   BioCyc; AHYD380703:G1G7B-96-MONOMER; -.
DR   UniPathway; UPA00908; UER00885.
DR   Proteomes; UP000000756; 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; 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.
PE   3: Inferred from homology;
DR   PRODOM; A0KEG8.
DR   SWISS-2DPAGE; A0KEG8.
KW   Complete proteome; Hydrolase; Reference proteome.
FT   CHAIN         1    496       Guanosine-5'-triphosphate,3'-diphosphate
FT                                pyrophosphatase.
FT                                /FTId=PRO_0000314491.
SQ   SEQUENCE   496 AA;  55133 MW;  3166C56CE0D4D7B0 CRC64;
     MHNSPLYAAI DLGSNSFHML VVREVAGALR TVTKVKRKVR LAAGLDPEFR LSRAAMERGW
     DCLRLFSEQL QDIPADNIRV VGTATLRLAT NVDEFLSEAE RVLNHSIEII SGEEEAKTIY
     EGVSWTSAGE GNRLVIDIGG ASTELVIGEH SEAKLLNSLH MGCVTWLNNH FGDGELSEAR
     FKQAIAAAKA VLEKVAEDYR ALGWRTCVGA SGTVQALQEI MLAQGKSERV TLPKLQELMG
     QAIACGKLDQ LQLEGLAAER LTVFPSGLAI LIAIFETLGI ESMTLAGGAL REGLIYGLLG
     NNHDCDARDR TADSLINRYQ LDKEHAERVR DTAVEAFNQL QPAWRLSKRY GRPILRYAAL
     LHEIGLCIEY KKAPQHAAYI IDNIDMPGFT PAQKKLLSAL LFNQRDEFKL EPLEKQGAVT
     GRQAIRLARI LRIALILCMR RTQGTVPRFT LEADEDALTL TLPSGWLDEH YLRASELRFE
     VERQQKMGWP TRLLEA
//

If you have problems or comments...

PBIL Back to PBIL home page