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Database: UniProt
Entry: A0A151JJA7_9VIBR
LinkDB: A0A151JJA7_9VIBR
Original site: A0A151JJA7_9VIBR 
ID   A0A151JJA7_9VIBR        Unreviewed;       706 AA.
AC   A0A151JJA7; A0A151L1B0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=ATY37_02755 {ECO:0000313|EMBL:KYN90129.1}, AUQ44_09360
GN   {ECO:0000313|EMBL:KYN25643.1};
OS   Vibrio cidicii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1763883 {ECO:0000313|EMBL:KYN25643.1, ECO:0000313|Proteomes:UP000075349};
RN   [1] {ECO:0000313|EMBL:KYN25643.1, ECO:0000313|Proteomes:UP000075346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2538-88 {ECO:0000313|Proteomes:UP000075346}, and 2756-81
RC   {ECO:0000313|EMBL:KYN25643.1};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KYN90129.1, ECO:0000313|Proteomes:UP000075349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2538-88 {ECO:0000313|EMBL:KYN90129.1}, and 2756-81
RC   {ECO:0000313|Proteomes:UP000075349};
RA   Tarr C.L., Gladney L.M.;
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:KYN25643.1}.
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DR   EMBL; LOMK01000001; KYN25643.1; -; Genomic_DNA.
DR   EMBL; LOBR01000007; KYN90129.1; -; Genomic_DNA.
DR   RefSeq; WP_061893589.1; NZ_LOBR01000007.1.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000075346; Unassembled WGS sequence.
DR   Proteomes; UP000075349; 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; 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:KYN25643.1}.
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          632..706
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   706 AA;  79618 MW;  2071C113AFA7F317 CRC64;
     MYLFDSLKDV AQEYLTEPQI EALRQSYVVA RDAHEGQTRS SGEPYIIHPV AVARILAEMR
     LDLETLQAAL LHDVIEDCDV SKEDLEAKFG QAVAELVDGV SKLDKLKFRD RKEAQAENFR
     KMVLAMVQDI RVILIKLADR THNMRTLGAL RPDKKRRIAR ETLEIYAPLA HRLGIHNIKT
     ELEELGFEAL YPNRYRVLKE VVKSARGNRK EMIQRIHSEI EGRLQDVGLN ARVLGREKNL
     FSIYNKMKTK EQRFHTIMDI YAFRVVVDTA DTCYRVLGQV HSLYKPRPGR MKDYIAVPKA
     NGYQSLHTSM VGPHGVPVEV QIRTEDMDQM ADKGVAAHWS YKGNGDRTGT TAQVKAQRWM
     QSLLELQQSA GNSFEFIENV KSDLFPDEIY VFTPKGRIVE LPVGATAVDF AYAVHTDVGN
     TCVGARVDRN PYPLSKALKN GQTIEIISAP GARPNAAWLN YVVTSRARTK IRQVLKTMRR
     EESITLGRRL LNHALGEHSL SDISPENMEH VLSDLKIASL DDLLAAIGLG ERMSIVIARR
     LLGDAEELTE VATPEGKPKK KLPIRGSEGL LLTFANCCHP IPDDSIIAHV SPGRGLVVHR
     ETCPNVRGYQ REPDKYMAVA WSEDYDQEFI AELKVDMQNH QGALAELTNV ISKTGSNIHG
     LSTEERDGRL YTVTVLLTTK DRVHLAGIMK KIRVMPSCSR VRRRKN
//
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