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Database: UniProt
Entry: F0BJ51_9XANT
LinkDB: F0BJ51_9XANT
Original site: F0BJ51_9XANT 
ID   F0BJ51_9XANT            Unreviewed;       723 AA.
AC   F0BJ51;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=XVE_4309 {ECO:0000313|EMBL:EGD07517.1};
OS   Xanthomonas vesicatoria ATCC 35937.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD07517.1, ECO:0000313|Proteomes:UP000003299};
RN   [1] {ECO:0000313|EMBL:EGD07517.1, ECO:0000313|Proteomes:UP000003299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD07517.1,
RC   ECO:0000313|Proteomes:UP000003299};
RX   PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA   Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA   Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA   Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA   Jones J.B.;
RT   "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT   and pepper.";
RL   BMC Genomics 12:146-146(2011).
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:EGD07517.1}.
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DR   EMBL; AEQV01000205; EGD07517.1; -; Genomic_DNA.
DR   RefSeq; WP_005996789.1; NZ_CP018725.1.
DR   AlphaFoldDB; F0BJ51; -.
DR   GeneID; 46981278; -.
DR   KEGG; xve:BJD12_07670; -.
DR   eggNOG; COG0317; Bacteria.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000003299; 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; 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;
FT   DOMAIN          65..164
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          406..467
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          651..723
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   723 AA;  80853 MW;  D96A581264967E6E CRC64;
     MNPGPTAQAT VATSPSSDPA IPEYVLHLER AASYLPKEQL PILRRAWEVG ATAHAGQTRK
     SGEPYITHPV AVAGVLAELG LDMESLIAAI LHDTIEDTPL TREELAAEFG EAVAELVDGV
     TKLDKLKFRD RQEAAAESFR KMLLAMSRDL RVIMIKLADR LHNMRTLGAQ STEARGRIAR
     ETLEIYAPIA QRLGMSLIKS ELQNLGFRAL YPWRHAIIEK HIRSQPVVRR ESMAQVEVQL
     SQRLAKEGLE HRLVSRIKTP WSIYSKMHEE NKSFDQVMDV FGFRLVVRTV ADCYHALGAV
     HATFKPLDGR FRDFIAIPKA NGYQSLHTVL FGPYGSPIEV QIRTEEMDLI AERGVAAHWT
     YKVGSASPNS AQSRAHDWIV ELIDSQRAAG SSLEFLDNVK VDLFPDEVYL FTPKGKILAL
     PRNSTALDFA YAVHTDVGNR AVASRVDKKL VPLRTKLVSG QAVEIITARS ATPKPQWLEF
     VVSSKARTAI RHQLKQLEHE DAVQLGHRML DRALEAMDSS LERLPKGRLD AFLNEHRYPR
     LEALLADVAL GNWMPTQAAQ ALMAYAELRG GGHSKHSHEK ILIDGSERGV ISFANCCQPI
     PGDEIMGYHT AGKGIVVHRL DCPNLAELRK SPERWVPIDW DSNVTGDYDT ALVVEVENRT
     GVLAQLAAAI AQSKSNIERV DYLDRDFNAA VLRFNIQVRD RRHLAEVMRR LRRLHVVQSV
     GRQ
//
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