ID A0A0G0FXY6_9BACT Unreviewed; 417 AA.
AC A0A0G0FXY6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=GTP pyrophosphokinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UR94_C0004G0036 {ECO:0000313|EMBL:KKP92175.1};
OS Parcubacteria group bacterium GW2011_GWA2_36_10.
OC Bacteria.
OX NCBI_TaxID=1618808 {ECO:0000313|EMBL:KKP92175.1, ECO:0000313|Proteomes:UP000034083};
RN [1] {ECO:0000313|EMBL:KKP92175.1, ECO:0000313|Proteomes:UP000034083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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}.
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:KKP92175.1}.
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DR EMBL; LBRC01000004; KKP92175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0FXY6; -.
DR STRING; 1618808.UR94_C0004G0036; -.
DR PATRIC; fig|1618808.3.peg.123; -.
DR Proteomes; UP000034083; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
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; 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; PF13328; HD_4; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..85
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 326..387
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 417 AA; 48149 MW; 1ED95AC0C203F9AE CRC64;
MKMDIPSITA GLLHDVPEDT DFSLDDVKNN FGKEVAELVA GVTKLGTLKY RGLERYAENL
RKMFLAMSKD LRIIIIKLAD RLHNMQTLEG VREEKRLRIA QETLEIYAPI ANRLGMFEIK
TRLEDLAFPY IYPSEYLWVS NLVKDRLKTE TKYIDKIQHL AQKDLVKNNI HYLQIKGRVK
SLFSIYQKLL HKGKDLNKVY DLIALRIIVP DVIDCYSVLG IIHKRWTPLK GRVKDYIAQP
KPNGYRSLHT SVFTEFGKIA EIQIRSQAMD EEAEFGIAAH SRYKELKNID SKKNPPTWVK
HLLEIQKSIT DNVEFIKHVK NDLFLNRIFV FTPKGDVIEL PENATPLDFA FHIHTDIGNK
CVGAKINEQM VSLNHALKSG DVVEILIDKN RKKPNPDWLN IVITTAAKDK IRNQLRK
//
