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Database: UniProt
Entry: A0A411WUA2_9BURK
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ID   A0A411WUA2_9BURK        Unreviewed;       759 AA.
AC   A0A411WUA2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:GGY52185.1, ECO:0000313|EMBL:QBI00218.1};
GN   ORFNames=EYF70_04650 {ECO:0000313|EMBL:QBI00218.1}, GCM10007387_37980
GN   {ECO:0000313|EMBL:GGY52185.1};
OS   Pseudoduganella albidiflava.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Pseudoduganella.
OX   NCBI_TaxID=321983 {ECO:0000313|EMBL:QBI00218.1, ECO:0000313|Proteomes:UP000292307};
RN   [1] {ECO:0000313|EMBL:GGY52185.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY52185.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [2] {ECO:0000313|EMBL:QBI00218.1, ECO:0000313|Proteomes:UP000292307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17472 {ECO:0000313|EMBL:QBI00218.1,
RC   ECO:0000313|Proteomes:UP000292307};
RA   Miess H., Frediansyhah A., Gross H.;
RT   "Draft Genome Sequences of Six Type Strains of the Genus Massilia.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:GGY52185.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY52185.1};
RA   Sun Q., Kim S.;
RL   Submitted (DEC-2022) 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   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; BMWV01000009; GGY52185.1; -; Genomic_DNA.
DR   EMBL; CP036401; QBI00218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411WUA2; -.
DR   KEGG; mali:EYF70_04650; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000292307; Chromosome.
DR   Proteomes; UP000628442; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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:QBI00218.1}.
FT   DOMAIN          93..192
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          434..495
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          684..756
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   759 AA;  84468 MW;  08F16702D752AB66 CRC64;
     MNLNSTESGI TERPVSRGRR SAARPDGDAG QPPAISTSPL AAPMTPAGVA TISHLTEKLA
     EYMSEADLKK VKEAYRFSDE MHLGQVRKSG EPYISHPIAV AEICADWKLD AQALMAALLH
     DVMEDQDVKK EELIERFGAP VAQLVDGLSK LEKIEFQSQI EAQAENFRKM LLAMASDVRV
     ILIKLADRLH NMRTLDVMAP AKKQRIAKET MEVYVPIAHR LGLNNIYREL QDLSFSHLYP
     LRYHVLAKAV KAARGNRREV VGKILDSVKN TLGMAGIHAE VYGREKTLYG IYKKMRSKHL
     TFSQVLDVYG FRVVVDSFSN CYVALGTLHS LYKPMPGKFK DYIAIRKLNG YQSLHTTLIG
     PYGTPVEFQI RTQEMHRTAE SGVAAHWLYK NSDANMTDMQ QRTHAWLQSL LDIQQQTGDS
     AEFLEHVKVD LFPDSVYVFT PKSKIIAMPR GATPIDFAYA IHTGIGDHTV SVTINGEPAP
     LRAELRNGDI VEVVTDPNSR PSPSWLSFVR TGKARSAIRH HLRTINLPES IGLGRQLLQQ
     ALAGISISPD LPEPLVERLL NESSAKSMDE LYADIGIGKR MAALVARHIF GLLGGESASV
     PIDHNSAADL DPVTIYGSEG VSVQLAPCCL PIPGDQIIGQ LRRDQGLQVH TSDCSVARRQ
     RQKEPDRWIA VKWGTELNRR FDSRIRLLIN NEKGILARVA AEIGESDGNI TFVGMDEDND
     HVLHQLRFTI QVKDRVHLAG LLRNVRKVTG VNRVSRERG
//
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