ID A0A1I1Q027_9GAMM Unreviewed; 708 AA.
AC A0A1I1Q027;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05660831_00901 {ECO:0000313|EMBL:SFD15272.1};
OS Thiohalospira halophila DSM 15071.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalospirales;
OC Thiohalospiraceae; Thiohalospira.
OX NCBI_TaxID=1123397 {ECO:0000313|EMBL:SFD15272.1, ECO:0000313|Proteomes:UP000198611};
RN [1] {ECO:0000313|EMBL:SFD15272.1, ECO:0000313|Proteomes:UP000198611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL3 {ECO:0000313|EMBL:SFD15272.1,
RC ECO:0000313|Proteomes:UP000198611};
RA de Groot N.N.;
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; FOMJ01000002; SFD15272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1Q027; -.
DR STRING; 1123397.SAMN05660831_00901; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000198611; 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:SFD15272.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198611};
KW Transferase {ECO:0000313|EMBL:SFD15272.1}.
FT DOMAIN 54..153
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 396..457
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 636..708
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 708 AA; 79298 MW; B9F675F5C9EEDB9D CRC64;
MSTAVQQEPV LLISDLCEQL EDYLEPEQVA EVYRAYLFGA EAHEGQQRLS GEPYIYHPLA
VAQILAELRL DHESLVAGVL HDTLEDTRVA KEDIAAAFSE EVAELVDGVS KLTQVHFSSK
AEAEAENFRK MMLAMARDLR VILIKLADRL HNMRTLGVMR PDKRRRIARE TLDIYAPIAN
RLGMNSLRLE LEDLGFRALH PMRYRILSKA VQRARGNRKE VVARIEGGLK ARLAEEGLEG
RVEGREKHLY SIYRKMRDKH LAFQEVFDVY AFRVVVDRVD TCYRVLGAVH NLYKPVPGRF
KDYIAIPKAN GYQSLHTVLF SPWGVPIEIQ IRTRDMDRVA EAGIAAHWLY KTGNEAHATV
AQTRAREWLR ELLEMQQNAG NSMEFLENVK VDLFPDEVYV FTPKGQIMEL PRGATAVDYA
YAVHSDVGNT CVGARIDRRL MPLNTRLLNG QTVEIVTAPG AHPNPAWLNF VITGKARTAI
RAYLKDLQAD EAVALGRRLL ERALSARGES LEGVDRQQLD RVVTELGAED PEGLFRDIGL
GRQLPALVAQ ALAPVAVGGG ETSQPLTVRG TEGMVVSFAK CCHPIPGDAI LGFMSAGRGL
VIHRRGCRNV VEDRHGPEKW MHVAWSDEAS GEFPVELRVE VANRRGVLAT VAATIAELEA
NIENVDVEDR DGVHSALLLT VSVRDRVHLA RIMRRIRKVE SVARITRY
//
