ID A0A077FIG7_9PSED Unreviewed; 702 AA.
AC A0A077FIG7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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 Name=spoT {ECO:0000313|EMBL:QGW75152.1};
GN ORFNames=GPJ81_00190 {ECO:0000313|EMBL:QGW75152.1}, PSAKL28_51650
GN {ECO:0000313|EMBL:AIL64305.1};
OS Pseudomonas alkylphenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL64305.1, ECO:0000313|Proteomes:UP000028931};
RN [1] {ECO:0000313|EMBL:AIL64305.1, ECO:0000313|Proteomes:UP000028931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KL28 {ECO:0000313|EMBL:AIL64305.1,
RC ECO:0000313|Proteomes:UP000028931};
RA Lee K., Lim J.Y., Hwang I.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QGW75152.1, ECO:0000313|Proteomes:UP000426235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Neo {ECO:0000313|EMBL:QGW75152.1,
RC ECO:0000313|Proteomes:UP000426235};
RA Ne Ville C.J., Enright D., Hernandez I., Dodsworth J., Orwin P.M.;
RT "Hybrid Genome Assemblies of two High G+C Isolates from Undergraduate
RT Microbiology Courses.";
RL Submitted (DEC-2019) 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; CP009048; AIL64305.1; -; Genomic_DNA.
DR EMBL; CP046621; QGW75152.1; -; Genomic_DNA.
DR RefSeq; WP_038615922.1; NZ_CP046621.1.
DR AlphaFoldDB; A0A077FIG7; -.
DR KEGG; palk:PSAKL28_51650; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000028931; Chromosome.
DR Proteomes; UP000426235; Chromosome.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:AIL64305.1};
KW Kinase {ECO:0000313|EMBL:QGW75152.1};
KW Transferase {ECO:0000313|EMBL:QGW75152.1}.
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; 78714 MW; 82C04266FDB13E1F CRC64;
MPSIDALADR LSTYLGADQV NLVRRAYFYA EQAHDGQRRR SGEAYVTHPL AVASILADMH
MDHQSLMAAM LHDVIEDTGI AKEALSSQFG ETVAELVDGV SKLTQMNFET KAEAQAENFQ
KMAMAMARDI RVILVKLADR LHNMRTLEVL SGEKRRRIAK ETLEIYAPIA NRLGMHSVRV
EFEDLGFKAM HPMRSARIYQ AVKRARGNRK EIVNKIEESL AHCLAVDGIE GEVSGRQKHL
YGIYKKMRGK RRAFNEIMDV YAFRIIVDKV DTCYRVLGAV HNLYKPLPGR FKDYIAIPKA
NGYQSLHTTL FGMHGVPIEI QIRTREMEEM ANNGIAAHWL YKSSDDEQPK GTHARARQWV
KGVLEMQQRA GNSLEFIESV KIDLFPDEVY VFTPKGRIME LPKGSTAVDF AYAVHTDVGN
SCIACRINRR LAPLSEPLQS GSTVEIVSAP GARPNPAWLN FVVTGKARTH IRHALKLQRR
SESISLGERL LNKVLNGFDS ALDKIPQERV QAMLSEYRLE QLEDMLEDIG LGNRMAYVVA
RRLLSSEGEQ LPTPEGPLAI RGTEGLVLSY AKCCTPIPGD PIVGHLSAGK GMVVHLENCR
NISEIRHNPE KCVQLSWAKD VTGEFNVELR VELEHQRGLI ALLASSVNAA DGNIEKISMD
ERDGRISVVQ LVVSVHDRVH LARVIKKLRA LTGVIRITRM RT
//
