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Database: UniProt
Entry: D7HFY6_VIBCL
LinkDB: D7HFY6_VIBCL
Original site: D7HFY6_VIBCL 
ID   D7HFY6_VIBCL            Unreviewed;       705 AA.
AC   D7HFY6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=VCRC385_01782 {ECO:0000313|EMBL:EFH73221.1};
OS   Vibrio cholerae RC385.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345074 {ECO:0000313|EMBL:EFH73221.1, ECO:0000313|Proteomes:UP000004696};
RN   [1] {ECO:0000313|Proteomes:UP000004696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC385 {ECO:0000313|Proteomes:UP000004696};
RA   Heidelberg J.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFH73221.1, ECO:0000313|Proteomes:UP000004696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC385 {ECO:0000313|EMBL:EFH73221.1,
RC   ECO:0000313|Proteomes:UP000004696};
RG   The Broad Institute Genome Sequencing Platform;
RA   Colwell R., Grim C.J., Young S., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA   Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Walk T., White J., Yandava C., Borodovsky M.,
RA   Heidelberg J., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Vibrio cholerae RC385.";
RL   Submitted (OCT-2009) 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; GG774560; EFH73221.1; -; Genomic_DNA.
DR   RefSeq; WP_001886099.1; NZ_GG774560.1.
DR   AlphaFoldDB; D7HFY6; -.
DR   PATRIC; fig|345074.23.peg.1004; -.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000004696; 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:SF36; 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:EFH73221.1}.
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          631..705
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   705 AA;  79512 MW;  CD12645787482BAE CRC64;
     MYLFDSLKDV AQEYLTEPQI EALRQSYVVA RDAHEGQTRS SGEPYIIHPV AVARILAEMR
     LDLETLQAAL LHDVIEDCDV TKEDLDAHFG SSVAELVDGV SKLDKLKFRD RKEAQAENFR
     KMVLAMVQDI RVILIKLADR THNMRTLGAL RPDKKRRIAR ETLEIYAPLA HRLGIHNIKT
     ELEELGFEAL YPNRYRVLKE VVKAARGNRK EMIQRIHSEI EGRLQDVGLS ARVVGREKNL
     FSIYNKMKTK EQRFHTIMDI YAFRIVVDTA DTCYRVLGQV HSLYKPRPAR MKDYIAVPKA
     NGYQSLHTSM VGPHGVPVEV QIRTEDMDQM ADKGVAAHWS YKANSERGGT TAQIKAQRWM
     QSLLELQQSA GNSFEFIENV KSDLFPDEIY VFTPKGRIVE LPMGATAVDF AYAVHTDIGN
     TCVGARVDRT PYPLSQSLKS GQTVEIISAP GARPNAAWLN YVVTSRARTK IRQVLKTMRR
     EDSVTLGRRL LNHALGEHSI NEIAPENISK VLSDLKIASM DDLLAAIGLG ELMSIVIARR
     LLGNADELTE PSKSGGNKNK LPIRGAEGIL LTFANCCHPI PDDHIIAHVS PGRGLVVHRE
     TCPNVRGYQK EPDKYMAVEW TKDYDQEFIT ELKVDMHNRQ GALAELTNVI SKTGSNIHGL
     STEERDGRLY TVTVLLTTKD RVHLAGIMRK IRTMPHALKV RRRKN
//
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