ID   A0A345DDN4_9BURK        Unreviewed;       736 AA.
AC   A0A345DDN4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:AXF86472.1};
DE            EC=3.1.7.2 {ECO:0000313|EMBL:AXF86472.1};
GN   Name=spoT {ECO:0000313|EMBL:AXF86472.1};
GN   ORFNames=DTO96_102226 {ECO:0000313|EMBL:AXF86472.1};
OS   Ephemeroptericola cinctiostellae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ephemeroptericola.
OX   NCBI_TaxID=2268024 {ECO:0000313|EMBL:AXF86472.1, ECO:0000313|Proteomes:UP000252182};
RN   [1] {ECO:0000313|Proteomes:UP000252182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F02 {ECO:0000313|Proteomes:UP000252182};
RA   Kim H.;
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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       {ECO:0000256|RuleBase:RU003847}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; CP031124; AXF86472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345DDN4; -.
DR   KEGG; hyf:DTO96_102226; -.
DR   Proteomes; UP000252182; Chromosome.
DR   GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; 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 {ECO:0000313|EMBL:AXF86472.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252182}.
FT   DOMAIN          60..159
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          401..462
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          658..731
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   736 AA;  82939 MW;  591D2634871615BA CRC64;
     MASSMAHKQH HADLIKVGLE NLFTQLSTYL SEADCARVRA AFLVADAAHL GQYRQTGEPY
     ITHPVAVATL CATWKLDTQS IMAALLHDVL EDTGTDKITL AHEFGAPVAN LVDGLSKLDK
     LHFDSKETQQ AESFRKMLLA MADDVRVILV KLADRLHNLS TMETLQWAKR RRIAQETLDI
     YAPIAHRLGL DGIYRQLQDL CFQQIHPMRA AVIEKALKRR RQQKRELFTK IVDQVQDAFA
     QSNLDADLSG REKNLASIYH KMKSKKLSLS KVLDVYAFRI IVPMRNDCYL ALGILHGLFN
     FVPGRFKDYI SLTKKNGYQS LHTTVLGPYG TPVEFQIRTY DMHRIAESGI ATHWLYKDND
     VSFSEVQKQS HTTLQSLFHI QQKTNDSIEF LEHIKVDLSP DAIYVFTPKS RILTLPRHAT
     VLDFAYSIHT DVGSHAVSGR INGVEAGLST ELRNGDRIEI ITNPTAAPHP SWLKWVKTGK
     ARSELRHYLK SQRVSESAHL GEQLFRQALD TIHLPYPDEA EKDIWDKLLA DSGCKTKEEL
     FSEIGLGIRP ANITAQRLLM VMPNNASNIV RTSEQSLVST GIERLVIRGD EANTITLSKC
     CHPIRGDAII GHLMRRQGLV VHTADCPNAR SQRAQDNLRW ISLEWDLQAE LADPFPVALQ
     IIAGDERGLL AKVASKISEA GANIEVVHSQ VLHNHVHVDI VIDVTDRVHL AQVFKNLRTL
     TRVEKIARRF GHKAKR
//