ID A0A1G6ZJH0_9GAMM Unreviewed; 729 AA.
AC A0A1G6ZJH0;
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=SAMN04488509_11446 {ECO:0000313|EMBL:SDE02894.1};
OS Aquimonas voraii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Aquimonas.
OX NCBI_TaxID=265719 {ECO:0000313|EMBL:SDE02894.1, ECO:0000313|Proteomes:UP000199603};
RN [1] {ECO:0000313|EMBL:SDE02894.1, ECO:0000313|Proteomes:UP000199603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16957 {ECO:0000313|EMBL:SDE02894.1,
RC ECO:0000313|Proteomes:UP000199603};
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; FNAG01000014; SDE02894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6ZJH0; -.
DR STRING; 265719.SAMN04488509_11446; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000199603; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:SDE02894.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199603}.
FT DOMAIN 61..160
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 413..474
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 657..729
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT COILED 669..696
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 729 AA; 81721 MW; 220B6C141F4AC78F CRC64;
MPPSALASAD APFDPCPEAI EALLVKLRPY LPAEQIPTVK RAYHVGAVAH DGQTRKSGEP
YITHPLAVAG ILAELGMDVE TLCAAILHDA LEDTQLGREA ISGEFGEAVA ELVDGVTKLD
KLSFRDRNEA MAESFRKMLL AMARDLRVIL IKLADRLHNM RTIGSMSADS RRRIARETLD
IYAPIAQRLG MNRIKSELQD LGFRAMHPWR HAVIARRIAQ QPVMRREAMA TIEAALSQKL
KQEGLKHRLV SRVKTPHSVY NKMRNEFKPR AGEVRAKRFE RVMDVFGFRV VVEQTMQCYH
ALGAVHALYK PVEARFRDFI AIPKANGYQS LHTVLFSPYG SHVEVQIRTE DMDLLAERGI
AAHWLYKTDA PQSSNNNAQN RARAWLSELL ESQQDAGSSL EFLENVKVDL FPDEVYIFSP
KGRIFALPRG ATVLDFAYAV HTDVGNRAVA SRIDKKLAPL RTRLTSGQTV EVITAPSAVP
NPQWLEFVVS SRARTAIRHH LKRLQHEDAV ELGHRMLEAA LDAIEASLER VPPAVLDHYL
QDNRLRRLED LLADIALGNR MPQQVALALT EGRLPGERRS TPRLEKIHIS GAGHGLLSFA
ACCRPLPGDE IMGYLSSGKG VVVHRMECPN LPELQKSPER WVPVDWDREV EGDFRAGLRV
EVLNKPGVLA QVAAAIAEAE SNIDNVEYQE RDLRMAVMHF GIEVKHRKHL ADVMRRVRKL
DVVLGIQRL
//
