ID   SPOT_SYNY3              Reviewed;         760 AA.
AC   P74007;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Probable 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=slr1325;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA18078.1; -; Genomic_DNA.
DR   PIR; S75517; S75517.
DR   AlphaFoldDB; P74007; -.
DR   SMR; P74007; -.
DR   IntAct; P74007; 3.
DR   STRING; 1148.gene:10498949; -.
DR   PaxDb; 1148-1653162; -.
DR   EnsemblBacteria; BAA18078; BAA18078; BAA18078.
DR   KEGG; syn:slr1325; -.
DR   eggNOG; COG0317; Bacteria.
DR   InParanoid; P74007; -.
DR   PhylomeDB; P74007; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000001425; 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..760
FT                   /note="Probable guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase"
FT                   /id="PRO_0000166576"
FT   DOMAIN          76..175
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          421..482
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   DOMAIN          685..759
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   REGION          585..614
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..599
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  86569 MW;  CA276EA2286358F7 CRC64;
     MNAVAALPTP TIHTTCAQDI HDIELPQWLE DCLQQWQREI EQGQDETTAP HCLICRAFCF
     AYDLHAQQRR KSGEPYIAHP VAVAGLLRDL GGDEAMIAAG FLHDVVEDTD ISIEQIEALF
     GEETASLVEG VTKLSKFNFS STTEHQAENF RRMFLAMAKD IRVIVVKLAD RLHNMRTLDA
     LSPEKQRRIA RETKDIFAPL ANRLGIWRFK WELEDLSFKY LEPDSYRKIQ SLVVEKRGDR
     ESRLETVKDM LRFRLRDEGI EHFELQGRPK HLYGIYYKMT SQDKAFEEIY DIAALRIIVE
     SKGECYRALS VVHDVFKPIP GRFKDYIGLP KPNRYQSLHT TVLGLTSRPL EIQIRTEEMH
     HVAEYGIAAH WKYKESGGSE NATLTSTDEK FTWLRQLLDW QSDLKDAQEY VENLKQNLFD
     DDVYVFTPKG EVISLARGAT PVDFAYRIHT EVGHHMKGAR VNGQWLGVDT RLKNGDIVEI
     VTQKNSHPSL DWLNFVVTPS ARHRIRQWFK RSRRDENILR GRELLEKELG KTGLEALLKS
     EPMQKTAERC NYQNVEDLLA GLGYGEITSN SVVNRLRENN VNNVKNSQSS QEVTLASSPQ
     VHPPTPPATG KDNSPIAGIE GLLYHIAGCC HPLPGEPIMG VVTRGARGIS IHRQGCHNLE
     QMDGDRLIPV RWNPNTNNHQ TYPVDIVIEA IDRVGVLKDI LSRLSDNHIN VRNADVKTHL
     GRPAIISLKI DIHDYQQLLG IMAKIKNMSD VMDLRRVISG
//