ID A0A418XK74_9PSED Unreviewed; 702 AA.
AC A0A418XK74;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D3879_06210 {ECO:0000313|EMBL:RJG12870.1};
OS Pseudomonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2320866 {ECO:0000313|EMBL:RJG12870.1, ECO:0000313|Proteomes:UP000284021};
RN [1] {ECO:0000313|EMBL:RJG12870.1, ECO:0000313|Proteomes:UP000284021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-6 {ECO:0000313|EMBL:RJG12870.1,
RC ECO:0000313|Proteomes:UP000284021};
RA Zhu H.;
RL Submitted (SEP-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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJG12870.1}.
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DR EMBL; QYUR01000002; RJG12870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418XK74; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000284021; Unassembled WGS sequence.
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:RJG12870.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 387..448
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 628..702
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 702 AA; 78770 MW; 438289C5332ACFA5 CRC64;
MPSIDALADR LSTYLGAEQV NLVRRAYFYA EQAHDGQRRR SGEAYVTHPL AVANILADMH
MDHQSLMAAM LHDVIEDTGI AKEALTAQFG ETVAELVDGV SKLTQMNFET KAEAQAENFQ
KMAMAMARDI RVILVKLADR LHNMRTLEVL AGEKRRRIAK ETLEIYAPIA NRLGMHSMRV
EFEELGFKAM HPMRSERIRQ AVKRARGNRK EIVNKIEESL THCLAREGME GEVIGREKHL
YGIYQKMRGK RRAFNEIMDV YAFRIIVDKV DTCYRVLGAV HNLYKPLPGR FKDYIAIPKA
NGYQSLHTTL FGMHGVPIEI QIRTRDMEEM ANNGIAAHWL YKSSEEDQPK GTHARARQWV
KGVLEMQQRA GNSLEFIESV KIDLFPDEVY VFTPKGRIME MPKGSTAVDF AYAVHTDVGN
SCIACRINRR LAPLSEPLQS GATVEIVTAP GARPNPAWLN FVVTGKARTH IRHALKLQRR
SESISLGERL LNKVLAGFNS HLDKLPTEQV RVVLGEYRLE LIEDLLEDIG LGNRMAYVVA
RRLLASEGEQ LPSAEGPLAI RGTEGLVLSY AKCCTPIPGD PIVGHLSAGK GMVVHLDNCK
NISEIRHNPE KCIQLSWAKD VVGEFNVELR IELEHQRGLI ALLASSVNAA DGNIEKISMD
ERDGRISVVQ LVVSVHDRVH LARVIKKLRA LKGVVHISRV RA
//
