ID A0A249KGQ5_9ACTN Unreviewed; 719 AA.
AC A0A249KGQ5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:ASY15993.1};
GN ORFNames=A1sIA56_03585 {ECO:0000313|EMBL:ASY15993.1};
OS Candidatus Planktophila sulfonica.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Planktophila.
OX NCBI_TaxID=1884904 {ECO:0000313|EMBL:ASY15993.1, ECO:0000313|Proteomes:UP000217215};
RN [1] {ECO:0000313|EMBL:ASY15993.1, ECO:0000313|Proteomes:UP000217215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IA-56 {ECO:0000313|EMBL:ASY15993.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
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; CP016773; ASY15993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249KGQ5; -.
DR KEGG; psuf:A1sIA56_03585; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000217215; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ASY15993.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000217215};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ASY15993.1}.
FT DOMAIN 48..145
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 383..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 647..719
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 719 AA; 79371 MW; C42A4A948EF263C4 CRC64;
MQTLPLIAPL IGALKEHHPQ ANTAEIERAF LVAENAHKGQ LRKSGEDYIT HPVAVTQILA
ELGLNETTLI ASLLHDTVED TPYSLDQLRS DFGDEIANLV DGVTKLDKLT YGPTAEAETV
RKMVIAMSRD IRVLVIKLAD RLHNARTWGF VSGESASRKA RETLDIYAPL AHRLGMNAIK
WELEDLSFGV LEPKKFEEIS RLVAERSPSR DALTAEVISA VESDLAKDEI SATVTGRKKH
FFSVYQKMVV RGRDFNDIYD LVGIRVLVND VRDCYAVLGS IHARWSPVPG RFKDYIAMPK
FNLYQSLHTT VIGPNGKAIE IQIRTYDMHS RAEFGIAAHW KYKQGGDPQS SSPEMLWLRQ
LHEWQKETED PSEFLEALRF DLGSPEVFVF TPKGSVVALP GGSTPVDFAF SVHTDVGLRC
AGAKVNGRLV PLESKLNNGD VIEIVTNKGE HAGPSRDWLN FVKSPRARSK IKAWFSKERR
EEAIDAGRES IARQMRKAGL PLQKIFAGHS LLELAHDMHY ADIDALYSAV GDGHVSAASI
IEKLVASMGA EDSHPEQTIE HIPTGVQAAK RTSSAIEVEG VDDVLVKLAR CCTPVPGDSI
MGFITKGSGI SVHRDDCINA SDLRTHQNER VVKVSWLAGA ASIFLVNIQV EALDRARLLA
DVTRTLSEQH VNILSAAVST SKDRVAISRF TFEMADAKHL DSVLAAVRGI EGVYDVYRT
//
