ID A0A1H3FH14_9PSED Unreviewed; 702 AA.
AC A0A1H3FH14;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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=SAMN05216287_4085 {ECO:0000313|EMBL:SDX90332.1};
OS Pseudomonas kuykendallii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1007099 {ECO:0000313|EMBL:SDX90332.1, ECO:0000313|Proteomes:UP000243778};
RN [1] {ECO:0000313|Proteomes:UP000243778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-59562 {ECO:0000313|Proteomes:UP000243778};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNNU01000007; SDX90332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3FH14; -.
DR STRING; 1007099.SAMN05216287_4085; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000243778; Unassembled WGS sequence.
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 Kinase {ECO:0000313|EMBL:SDX90332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243778};
KW Transferase {ECO:0000313|EMBL:SDX90332.1}.
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; 78544 MW; 3D863C5493F6C7DE CRC64;
MASIDTLAER LSTYLGADQV NLVRRAYFYA EQAHDGQRRR SGEAYVTHPL AVANILADMH
MDHQSLMAAM LHDVIEDTGI AKEALIAQFG ETVADLVDGV SKLTQMNFET KAEAQAENFQ
KMAMAMARDI RVILVKLADR LHNMRTLEVL SGEKRRRIAK ETLEIYAPIA NRLGMHAMRV
EFEDLGFKAM HPMRSGLIAK AVKKARGNRK EIVNKIEESL THCLQRDELE GEVVGREKHL
YSIYQKMRGK HKAFNEIMDV YAFRIIVDKV DTCYRVLGAV HSLYKPLPGR FKDYIAIPKA
NGYQSLHTTL FGMHGVPIEI QIRTREMEEM ANNGIAAHWL YKSSDDEQPK GTHARARQWV
KGVLEMQQRA GNSLEFIESV KIDLFPDEVY VFTPKGRIME LPKGSTAVDF AYAVHTDVGN
SCIACRINRR LAPLSQPLES GETVEIVSAP GARPNPAWLN FVVTGKARTH IRHALKQQRR
SESISLGERL LNKVLAGFDS HLDKIAAERV RGVLAEYRME VLEDLLEDIG LGNRMAYVVA
RRLLASEGEQ PQSAEGPLAI RGTEGLVLSY AKCCTPIPGD PIVGHLSAGK GMVVHLESCK
NIAEIRNNPE KCVQLSWAKD VTGEFNVELR VELEHQRGLI ALLAGSVNAA DGNIEKIGMD
ERDGRISVVQ LVISVHDRVH LARVIRKLRT LMGVVRITRV RA
//
