ID S2EYW1_9PSED Unreviewed; 701 AA.
AC S2EYW1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=PG5_30320 {ECO:0000313|EMBL:EPA96301.1};
OS Pseudomonas sp. G5(2012).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1268068 {ECO:0000313|EMBL:EPA96301.1, ECO:0000313|Proteomes:UP000014290};
RN [1] {ECO:0000313|EMBL:EPA96301.1, ECO:0000313|Proteomes:UP000014290}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G5(2012) {ECO:0000313|Proteomes:UP000014290};
RA Park S., Lee J.-H., Cho Y.-J., Chun J., Hur H.-G.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain G5, Isolated from a
RT Traditional Indigo Fermentation Dye Vat.";
RL Submitted (MAR-2013) 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:EPA96301.1}.
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DR EMBL; APIO01000044; EPA96301.1; -; Genomic_DNA.
DR RefSeq; WP_008062824.1; NZ_APIO01000044.1.
DR AlphaFoldDB; S2EYW1; -.
DR GeneID; 72191949; -.
DR PATRIC; fig|1268068.3.peg.2893; -.
DR eggNOG; COG0317; Bacteria.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000014290; Unassembled WGS sequence.
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;
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 627..701
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 701 AA; 78569 MW; B83C50307AF98273 CRC64;
MPSIDALADR LSTYLGKDQV NLVRRAYFYA EQAHDGQRRR SGEAYVTHPL AVANILADMH
MDHQSLMAAM LHDVIEDTGI AKEALQAQFG ETVAELVDGV SKLTQMNFET KAEAQAENFQ
KMAMAMARDI RVILVKLADR LHNMRTLEVL SGEKRRRIAK ETLEIYAPIA NRLGMHAIRI
EFEDLGFKAM HPMRSARIYQ AVKRARGNRK EIVNKIEESL SHCLAIDGIQ GEVSGRQKHL
YGIYKKMRGK RRAFNEIMDV YAFRIIVDKV DTCYRVLGAV HNLYKPLPGR FKDYIAIPKA
NGYQSLHTTL FGMHGVPIEI QIRTREMEEM ANNGIAAHWL YKSSGDEQPK GTHARARQWV
KGVLEMQQRA GNSLEFIESV KIDLFPDEVY VFTPKGRIME LPKGSTAVDF AYAVHTDVGN
SCIACRINRR LAPLSEPLQS GSTVEIVSAP GARPNPAWLN FVVTGKARTH IRHALKLQRR
SESISLGERL LNKVLNGFDS SLEKIPAERV KAMLAEYRLE LIEDLLEDIG LGNRMAYVVA
RRLLGEGEQL PSPEGPLAIR GTEGLVLSYA KCCTPIPGDP IVGHLSAGKG MVVHLDNCRN
ISEIRHNPEK CIQLSWAKDV TGEFNVELRV ELEHQRGLIA LLASSVNAAD GNIEKISMDE
RDGRISVVQL VVSVHDRVHL ARVIKKLRAL TGVIRITRMR A
//