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   27-MAR-2024, entry version 141.
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; Aquificota; 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 aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC       is a mediator of the stringent response that coordinates a variety of
CC       cellular activities in response to changes in nutritional abundance.
CC       This enzyme catalyzes the degradation of ppGpp into GDP. It may also be
CC       capable of catalyzing the synthesis of ppGpp (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC         H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, 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: step
CC       1/1.
CC   -!- SIMILARITY: Belongs to the RelA/SpoT family. {ECO:0000305}.
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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   AlphaFoldDB; O67012; -.
DR   SMR; O67012; -.
DR   STRING; 224324.aq_844; -.
DR   EnsemblBacteria; AAC06975; AAC06975; aq_844.
DR   KEGG; aae:aq_844; -.
DR   PATRIC; fig|224324.8.peg.658; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_0; -.
DR   InParanoid; O67012; -.
DR   OrthoDB; 9805041at2; -.
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; cd04876; ACT_RelA-SpoT; 1.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RSH; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR004811; RelA/Spo_fam.
DR   InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   NCBIfam; TIGR00691; spoT_relA; 1.
DR   PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF19296; RelA_AH_RIS; 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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..696
FT                   /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase"
FT                   /id="PRO_0000166567"
FT   DOMAIN          49..145
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          383..446
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          623..696
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-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
//