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Database: UniProt
Entry: A0A094PIE4_9ACTN
LinkDB: A0A094PIE4_9ACTN
Original site: A0A094PIE4_9ACTN 
ID   A0A094PIE4_9ACTN        Unreviewed;       744 AA.
AC   A0A094PIE4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:KGA10767.1};
GN   ORFNames=GM46_4975 {ECO:0000313|EMBL:KGA10767.1};
OS   actinobacterium acAcidi.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA10767.1, ECO:0000313|Proteomes:UP000029305};
RN   [1] {ECO:0000313|EMBL:KGA10767.1, ECO:0000313|Proteomes:UP000029305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT   "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT   sequencing.";
RL   Submitted (MAY-2014) 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. {ECO:0000256|ARBA:ARBA00025704}.
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:KGA10767.1}.
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DR   EMBL; JNSG01000042; KGA10767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094PIE4; -.
DR   PATRIC; fig|1504320.4.peg.999; -.
DR   Proteomes; UP000029305; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase 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; 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; 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; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGA10767.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KGA10767.1}.
FT   DOMAIN          62..161
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          397..458
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          660..734
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   744 AA;  82764 MW;  D22B609D312B175E CRC64;
     MSTTSRVLPW RRNQSAVNQE LLPLLSAFKQ NHPKASITQV NAAYAMASSA HKHQSRMSGE
     LYVSHPLAVA RIVAEIGLDE VSLVAALLHD AVEDTEITLA DVESNFGAEI AGIVDGLTKL
     ERLQFDSREA QQAATMRKML VAMARDLRVL IIKLADRLHN MRTIASAPID KQRRVAQETL
     DIYAPLAHRL GMQEMKQQLE DLSFAALYPK RYAELDYLVS TRAPERDVYL AKALGQVDGW
     LNEVNIKAEL TARGKHLWSL YEKMVQKGRD FDEIFDLMAV RIIVDSVKDC YSALGCIHGH
     WKPVVGRFKD YIAMPKFNLY QSLHTTVIGP GGKPIEVQIR SRDMHQRAEW GVASHWSYKD
     GIASTDIDWL NRIIDWQDEV SDPRQFLESL KTDLDQDELF VFTPKGRVVS LPVNATPVDF
     AYAVHTEVGH SCIGARVNGR LVPLDSLLNS GDTCEVLTST ADEPGPMEEW INSVVSPKAK
     SKIKQWFSRE RLEDLVETGR DDLVEQIRHL GMPVQQVLES EAFNLEMSAM NYSDATALFL
     AIGEGHVAAD SFANRLSRAF GDGEFGEQLS VGMRFDSAGL DSIQQAGIHV EGLDQSIVRL
     SKCCTPVPGD EIIGFIVADR SVNVHRSDCS TAIMAISNNV GRVVDVEWSG NLRGATFVAA
     VEVVALDRSR LLRDVANALS EEHVNIVACT TQTGQDRVAK MRFEFEFADP SHLQSVLRTI
     KRIDSVYDAY RVMSGEHPAS NLPV
//
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