ID   A0A1D9H1X0_9BURK        Unreviewed;       740 AA.
AC   A0A1D9H1X0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:AOY93650.1};
GN   ORFNames=BKK79_18940 {ECO:0000313|EMBL:AOY93650.1};
OS   Cupriavidus sp. USMAA2-4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY93650.1, ECO:0000313|Proteomes:UP000178101};
RN   [1] {ECO:0000313|EMBL:AOY93650.1, ECO:0000313|Proteomes:UP000178101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY93650.1,
RC   ECO:0000313|Proteomes:UP000178101};
RA   Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT   "Complete genome sequences of three Cupriavidus strains isolated from
RT   various Malaysian environments.";
RL   Submitted (OCT-2016) 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; CP017748; AOY93650.1; -; Genomic_DNA.
DR   RefSeq; WP_071038235.1; NZ_CP017748.1.
DR   AlphaFoldDB; A0A1D9H1X0; -.
DR   STRING; 876364.BKK79_18940; -.
DR   KEGG; cuu:BKK79_18940; -.
DR   Proteomes; UP000178101; Chromosome 1.
DR   GO; GO:0016301; F:kinase 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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   Kinase {ECO:0000313|EMBL:AOY93650.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000178101};
KW   Transferase {ECO:0000313|EMBL:AOY93650.1}.
FT   DOMAIN          409..470
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          669..740
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   740 AA;  82089 MW;  C5B0D467501B9AEE CRC64;
     MVTPTELPGQ VAGTPDAGLV VRALAFVRAR GAGAELPTGE SVLSHAEGML RILDGLRVDD
     AARAAACLFP VAAYVPGCEA DIEADFGEEV ARLVKGVRQL LRIGAIAVTQ AEAQEPGKNE
     REARHEQVEA LRKMLLAFAQ DIRVVLVRLA SRLQTLRWLA QAKRAPLPGV ARETLDIYAP
     LANRLGIWQM KWELEDLAFR FEQPDTYKRI ARLLDEKRIE REGYIASAIA RLQAELAAAG
     IRADVSGRPK HIFSIWKKMR GKELDFADLY DVRAFRVIVD DIKDCYAVLG IVHHIWQPIP
     REFDDYISRP KPNGYKSLHT VVIGDDGRAF EVQIRTQEMH HFAEYGVAAH WRYKEAGNRG
     YSGQFSADER YDEKIAWVRQ LLAWKDDADH TVAHEDSPWE QLKHAAIDDH IYVLTPQARV
     VALPQGATPV DFAYYLHTDL GHRCRGARVD GAMVPLNTPL KNGQTVEVVA VKQGGPSRDW
     LNPELGYLAS GRARAKVRAW FNALDSQETI AQGRAQVDKT LQREGKTAVN LDDLAARLGF
     KAPDELFAAV AKEEFSLRHV EQALRHPAGE VQPHISEEDA VTKKSRATSV ARGAKSGVLV
     VGVDSLMTQM SRCCKPAPPD DIVGFVTRGR GVSIHRRTCP TFLQLSARAP ERVIQTEWGK
     KSDAVYPVDI HVEAVDRQGL LRDISEVLSR EKINVTGVKT LSSKGVARMQ FTAEVAEATQ
     LQRALALIED VVGVLQAKRK
//