(data stored in ACNUC7421 zone)

SWISSPROT: GPPA_PSEHT

ID   GPPA_PSEHT              Reviewed;         497 AA.
AC   Q3IDD5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   08-MAY-2019, entry version 71.
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=PSHAa0115;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI85224.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CR954246; CAI85224.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011326842.1; NC_007481.1.
DR   SMR; Q3IDD5; -.
DR   STRING; 326442.PSHAa0115; -.
DR   EnsemblBacteria; CAI85224; CAI85224; PSHAa0115.
DR   KEGG; pha:PSHAa0115; -.
DR   PATRIC; fig|326442.8.peg.114; -.
DR   eggNOG; ENOG4105C9X; Bacteria.
DR   eggNOG; COG0248; LUCA.
DR   HOGENOM; HOG000258672; -.
DR   KO; K01524; -.
DR   OrthoDB; 1862004at2; -.
DR   BioCyc; PHAL326442:PSHA_RS00585-MONOMER; -.
DR   UniPathway; UPA00908; UER00885.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IDD5.
DR   SWISS-2DPAGE; Q3IDD5.
KW   Complete proteome; Hydrolase; Reference proteome.
FT   CHAIN         1    497       Guanosine-5'-triphosphate,3'-diphosphate
FT                                pyrophosphatase.
FT                                /FTId=PRO_0000194285.
SQ   SEQUENCE   497 AA;  54968 MW;  C7E1CC2B2FEB8A26 CRC64;
     MGQLKPQKNV YAVIDLGSNS FHMLIAKSIA GGLQTIGRVK RKVRLAAGLD IDNVLSSEAM
     HRGWECLALF AERLQDIPKQ NITIVATATL RLASNADVFK AQAEKILGHK VNVISGELEA
     RTIYKGVAHT SSCTGSQLVI DIGGASTEVI IGKNFDALLY KSLNIGCVTY LERYFKDCKL
     SNANFNTAIK AARTVIDEIA SEYKVKGWQI ASGASGTVQA IQEIMIAQNL DELLTLEKLY
     TIKKQSIAYK TIAALDLPGL SEDRRLVFVS GLAILIALFE SLEIEKMGLA GGALREGVLY
     SMLPELHNSD IRKRTIDGFI DRYHVDQKQA SRVASLVLNL ASEVNESWPI KALNGLPLLT
     AVAQLHEIGL LIEYKQYHKH SAYILKNTEM PGFSQSEHKV IVAVAKGHRS DLQKGYFDSL
     GANSVLAQYL VRLIRIAVIL CMRRQDDVLP EFAITVKDDV LNLQFENDWL KNHPLMASEL
     QQESKQQAKL GWKLIVN
//

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