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Database: UniProt
Entry: A0A411WWD5_9BURK
LinkDB: A0A411WWD5_9BURK
Original site: A0A411WWD5_9BURK 
ID   A0A411WWD5_9BURK        Unreviewed;       747 AA.
AC   A0A411WWD5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE            EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE   AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE   AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE   AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN   Name=relA {ECO:0000313|EMBL:GGY48123.1};
GN   ORFNames=EYF70_09770 {ECO:0000313|EMBL:QBI01101.1}, GCM10007387_32820
GN   {ECO:0000313|EMBL:GGY48123.1};
OS   Pseudoduganella albidiflava.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Pseudoduganella.
OX   NCBI_TaxID=321983 {ECO:0000313|EMBL:QBI01101.1, ECO:0000313|Proteomes:UP000292307};
RN   [1] {ECO:0000313|EMBL:GGY48123.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY48123.1};
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:QBI01101.1, ECO:0000313|Proteomes:UP000292307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17472 {ECO:0000313|EMBL:QBI01101.1,
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:GGY48123.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KCTC 12343 {ECO:0000313|EMBL:GGY48123.1};
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   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC       1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; BMWV01000007; GGY48123.1; -; Genomic_DNA.
DR   EMBL; CP036401; QBI01101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411WWD5; -.
DR   KEGG; mali:EYF70_09770; -.
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; 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; 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:SF40; GTP PYROPHOSPHOKINASE; 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; 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; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:QBI01101.1}.
FT   DOMAIN          416..477
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          676..747
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   747 AA;  82501 MW;  BA73D053F52AA118 CRC64;
     MVSIAALNSA TSEQLVLGLS SDDGARVLAA LDFASAAYAG KQCTSGQPAL DFAVGAASTL
     ALLNTDAATR IAALLFELCL LDPAQGIAIE PKFGKEVADL VIGVHQLIRL RELTQGSPAA
     TRGKNAAQQA VAQMETLRKM LLAMASDMRV VLVRLASCCS TLRWFADQKI FNEMTRAYGR
     ETLDLYAPLA NRLGIWQIKW ELEDLSFRFI EPENYKRIAK MLEEKRMMRE SFVTQSIARL
     QSELAAAGIQ AEVFGRPKHI YSIWNKMRGK ELDFTELYDV RAFRVIVPDV KTCYTVLGLV
     HNIWTPIPKE FDDYISRPKP NGYQSLHTVV TADDGRPLEV QIRTQEMHSF AEYGVAAHWR
     YKEEGNSSFQ GQKYDEKIAW LRQLLAWKTD VADAVVGQEE LQREWVEKLK EAALDDRIFV
     LTPQARVLEL PVGATPIDFA YHLHSDVGHR CRGARVDGVM VPLNTPLKSG QTCEIITAKG
     APGTAGPSRD WLSPGYAVSN RTRAKVRAWF HAIDVQETLS HGRSLVEKSL QREGKTAVNL
     ETLAQKLGFA KVDELFLAVG KEEFSLRHVE HALHDNAEPA PPEDAVVLNK SRASSTEQGA
     KSGVLVVGTE GLMTQLARCC KPAPPDPIVG FVTRGKGVSI HRLSCKNFAE MRIKAPERVI
     VTEWGDGQRE TVYPVDLFVL AGDRQGLLRD ISEVFSREKI NVIGVNTQSA KGQARMTFTA
     EIGSTAQVHK ALAAISEVTG VLEARRA
//
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