GenomeNet

Database: UniProt
Entry: S2EYW1_9PSED
LinkDB: S2EYW1_9PSED
Original site: S2EYW1_9PSED 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system