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Database: UniProt
Entry: SPOT_AQUAE
LinkDB: SPOT_AQUAE
Original site: SPOT_AQUAE 
ID   SPOT_AQUAE              Reviewed;         696 AA.
AC   O67012;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   05-JUN-2019, entry version 124.
DE   RecName: Full=Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase;
DE            EC=3.1.7.2;
DE   AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase;
DE            Short=(ppGpp)ase;
GN   Name=spoT; OrderedLocusNames=aq_844;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5-'
CC       diphosphate) is a mediator of the stringent response that
CC       coordinates a variety of cellular activities in response to
CC       changes in nutritional abundance. This enzyme catalyzes the
CC       degradation of ppGpp into GDP. It may also be capable of
CC       catalyzing the synthesis of ppGpp (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate +
CC         GDP + H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:77828; EC=3.1.7.2;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP:
CC       step 1/1.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
DR   EMBL; AE000657; AAC06975.1; -; Genomic_DNA.
DR   PIR; A70373; A70373.
DR   RefSeq; NP_213573.1; NC_000918.1.
DR   RefSeq; WP_010880511.1; NC_000918.1.
DR   SMR; O67012; -.
DR   STRING; 224324.aq_844; -.
DR   EnsemblBacteria; AAC06975; AAC06975; aq_844.
DR   GeneID; 1193554; -.
DR   KEGG; aae:aq_844; -.
DR   PATRIC; fig|224324.8.peg.658; -.
DR   eggNOG; ENOG4105CWR; Bacteria.
DR   eggNOG; COG0317; LUCA.
DR   HOGENOM; HOG000018299; -.
DR   InParanoid; O67012; -.
DR   KO; K01139; -.
DR   OMA; HYYSIYQ; -.
DR   OrthoDB; 204079at2; -.
DR   BioCyc; AAEO224324:G1G15-599-MONOMER; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RelA_SpoT; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR004811; RelA/Spo_fam.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   TIGRFAMs; TIGR00691; spoT_relA; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Manganese; Reference proteome.
FT   CHAIN         1    696       Guanosine-3',5'-bis(diphosphate) 3'-
FT                                pyrophosphohydrolase.
FT                                /FTId=PRO_0000166567.
FT   DOMAIN       49    145       HD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01175}.
FT   DOMAIN      383    446       TGS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01228}.
FT   DOMAIN      623    696       ACT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01007}.
SQ   SEQUENCE   696 AA;  80570 MW;  825F3FE6A556FF15 CRC64;
     MSKLGEVSLE EDLEKLLSHY PQHAEEIQRA YEFAKEKHGE QKRKTGEPYI IHPLNVALKL
     AELGMDHETI IAALLHDTLE DTDTTYEEIK ERFGERVAKL VEGVTKIGKI KYKSEQAENY
     RKLILATAED PRVILLKLSD RLDNVKTLWV FREEKRKKIA KETMEIYAPL AHRLGVWSIK
     NELEDWAFKY LYPEEYEKVR NFVKESRKNL EEYLRKYVIP KVRKELEKYG IEAEIKYRSK
     HYYSIWEKTR RKGIRLEDVH DILGVRIIVN TVPECYTVLG IIHSLFRPVP GKFKDYISLP
     KPNLYQSLHT TVIADKGKLV EFQIRTWEMH ERAEKGIASH WAYKEGKNPS DAGVYSWLRE
     LVESIQGSTN PSEVLENLKS NLFFEEVFVF TPKGDLVVLP KGSTPVDLAY KIHTEVGNHC
     AGAKSNGRIV PLNYELKSGD VVEIITNPNK SPSYEWLSFV KTSRARNKIK QFLKKQERER
     YLSEGKRILE RIREKLGLSH EDLINKIRER VRFDTEEELL LALGKRKISS ANLIKLIFPK
     KKEEKEERRG SSTVFLEDLS NIKHEVAKCC KPIPGDEILG VITRTKGLVL HEKSCSNLKN
     VLRLNPEKVK EVQLQASGYF QTDIRVVASD RIGLLSDITK VISESGSNIV SSMTNTREGK
     AVMDFTVEVK NKEHLEKIMK KIKSVEGVKI CKRLYH
//
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