ID   G7LMG2_9GAMM            Unreviewed;       699 AA.
AC   G7LMG2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=guanosine-3',5'-bis(diphosphate) 3'-diphosphatase {ECO:0000256|ARBA:ARBA00024387};
DE            EC=3.1.7.2 {ECO:0000256|ARBA:ARBA00024387};
GN   ORFNames=BrE312_4400 {ECO:0000313|EMBL:EHD23715.1};
OS   Brenneria sp. EniD312.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Brenneria.
OX   NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD23715.1};
RN   [1] {ECO:0000313|EMBL:EHD23715.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EniD312 {ECO:0000313|EMBL:EHD23715.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA   Glasner J., Perna N., Woyke T.;
RT   "Complete sequence of Brenneria sp. EniD312.";
RL   Submitted (JUL-2011) 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   -!- 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         Evidence={ECO:0000256|ARBA:ARBA00024273};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC       1/1. {ECO:0000256|ARBA:ARBA00024329}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; CM001230; EHD23715.1; -; Genomic_DNA.
DR   RefSeq; WP_009115010.1; NZ_CM001230.1.
DR   AlphaFoldDB; G7LMG2; -.
DR   STRING; 598467.BrE312_4400; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000002759; 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 {ECO:0000313|EMBL:EHD23715.1}.
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          385..446
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          625..699
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   699 AA;  79075 MW;  C0D6A8C014A4A7EE CRC64;
     MYLFESLNLL IQRYLPEEQI KRLRQAYLVA RDAHEGQTRS SGEPYITHPV AVACILAEMR
     LDYETLMAAL LHDVIEDTPA TYQDMEQLFG KSVAELVEGV SKLDKLKFRD KKEAQAENFR
     KMIMAMVQDI RVILIKLADR THNMRTLGSL RPDKRRRIAR ETLEIYSPLA HRLGIHHLKT
     ELEELGFEAL YPNRYRVIKE VVKAARGNRK EMIQKILAEI EGRLTEAGIA CRVSGREKHL
     YSIYCKMHLK EQRFHSIMDI YAFRVIVKEL DTCYRVLGQV HSLYKPRPGR VKDYIAIPKA
     NGYQSLHTSL IGPHGVPVEV QIRTDDMDQM AEMGVAAHWA YKEGESSTTA QVRAQRWMQS
     LLELQQSAGS SFEFIESVKS DLFPDEMYVF TPEGRIVELP AGATPVDFAY AVHTDIGHAC
     VGARVDRQPY PLSQSLTSGQ TVEIITAPGA RPNAAWLNFV VSSRARAKIR QMLKNLKRDD
     SVSLGRRLLN HALGSGRKLS DIPPKNIQLE LDRMKLATLD DLMAEIGLGN AMSVVVAKNL
     LNEQSQLDNT GPRKLPIKGA DGVMVSFAKC CRPIPGDPII AHVSPGKGLV IHHESCRNIR
     GYQKEPEKFM AVEWDKVTEQ EFIAEIKVDM FNHQGALANL AAAINTANSN IQSINTEERD
     GRVYSAFIRL TTLDRVHLAN VMRKIRVMPD VIKVNRNRN
//