ID A0A0W1RT53_9GAMM Unreviewed; 729 AA.
AC A0A0W1RT53;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AUR63_01295 {ECO:0000313|EMBL:KTG16729.1};
OS Guyparkeria sp. XI15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Thioalkalibacteraceae; Guyparkeria.
OX NCBI_TaxID=1766620 {ECO:0000313|EMBL:KTG16729.1, ECO:0000313|Proteomes:UP000053033};
RN [1] {ECO:0000313|Proteomes:UP000053033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XI15 {ECO:0000313|Proteomes:UP000053033};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloferax marisrubri sp. nov., isolated from the Discovery deep brine-
RT seawater interface in the Red Sea.";
RL Submitted (DEC-2015) 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:KTG16729.1}.
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DR EMBL; LOPX01000014; KTG16729.1; -; Genomic_DNA.
DR RefSeq; WP_058574951.1; NZ_LOPX01000014.1.
DR AlphaFoldDB; A0A0W1RT53; -.
DR STRING; 1766620.AUR63_01295; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000053033; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000053033}.
FT DOMAIN 67..166
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 408..469
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 657..729
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 729 AA; 81287 MW; A07F347162508D42 CRC64;
MDVDSGQTGT PTAAPSAESH LTDVFFAPLA QHLAEYLDSA DIARIRTAFE FGAEAHAGQT
RKSGEPYISH PIAVAHILAD LRMDEATLVA AILHDVVEDT DIAHDQIVAE FGDEVAHLVD
GVSKLAQIRF KSKAEAQAAN FRKMMMAMVE DVRVILIKLA DRLHNMRTLG VMRPDKRRRI
ARETLDIYTP IANRLGLNAI RHELEDLGFA SLHPLRHRIL SEAVRRARGN RKEIVAGIQE
RFEQRFTHES LTADILAREK RPYSIYRKMQ SKRLSFREVF DVFAVRVLVE SVDDCYRALG
IVHNLYKPLP GRFKDYIAIP KANGYQSLHT ILFGPHGIPL EVQIRTHEMH QFAESGIAAH
WLYKAQGDHG SVTQTRAREW LRDLLEIQQK AGNPQEFLES VKVDLFPDEV YVFTPMGEII
ELPRRATAVD FAYAIHTDVG NTCVACKIDR RFAPLSTPLE SGQTVEVITA PGAVPNPSWL
SFVVTARARA NIRAYLKHLQ DAEAIRLGHR LLSKAMTAEG CDIEDLDESR VDKLLREYHQ
ESFNDLLREI GLGNRMAPLV VRLLKAEAGK IELTEPEGGL PPEQAPVIIS GTEGLVVSFA
GCCHPVPGDS VVGFLSTGRG IVVHRQGCPN AADAGEHPER WLAVDWEQQP SGEYQSQISI
HANNVRGGLA RIAAAVSDAG SDIDDVRFDD RDVNLTIIDI TVRVTDRTHL ARVMRSIKQL
RDVVRVSRH
//