ID A0A1C7I8Q1_9FIRM Unreviewed; 769 AA.
AC A0A1C7I8Q1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=A4V09_09830 {ECO:0000313|EMBL:ANU76036.1};
OS Blautia pseudococcoides.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1796616 {ECO:0000313|EMBL:ANU76036.1, ECO:0000313|Proteomes:UP000092574};
RN [1] {ECO:0000313|Proteomes:UP000092574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL58 {ECO:0000313|Proteomes:UP000092574};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-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; CP015405; ANU76036.1; -; Genomic_DNA.
DR RefSeq; WP_065542213.1; NZ_CP065312.1.
DR AlphaFoldDB; A0A1C7I8Q1; -.
DR STRING; 1796616.A4V09_09830; -.
DR KEGG; byl:A4V09_09830; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000092574; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ANU76036.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092574};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ANU76036.1}.
FT DOMAIN 78..178
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 426..487
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 695..769
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 769 AA; 87187 MW; FB707E579B09BDBC CRC64;
MEKSKEAALQ DDEIAKIKKA DASVKTMEDF TSPSVLYEEL ISSVRKYHPS TDISMIEKAY
RIARDAHEGQ VRKSGEPYII HPLCVGIILA DLELDKETIV AGLLHDVVED TVMTTEEITQ
EFGAEVALLV DGVTKLGQLN YSADKVEVQA ENLRKMFLAM AKDIRVILIK LADRLHNMRT
LKYMPPHKQK EKARETMDIY APIAQRLGIS KVKIELDDLS LKYLEPEVYY DLVEKINLRK
SEREAFVSGI VNGVREQIEY AGIHAQIDGR VKHFFSIYKK MVNQDKTLDQ IYDLFAVRII
VDTVKDCYAS LGIIHEMYKP IPGRFKDYIA MPKPNMYQSL HTTLIGPNGQ PFEIQIRTFE
MHRTAEYGIA AHWKYKEASG SSKASVTQQE EEKMSWLRQI LEWQRDMSDN KEFLSLLKSD
LDLFSESVYC FTPAGDVKTL PNGSTPIDFA YNVHSAVGNK MVGARVNGKL VPIDYVIKNG
DRIEIITSQN SKGPSRDWLK VVKSTQAKNK INQWFKQELK EDNILKGKDM LAQYAKLKGI
GLGNLTKPKY LESVMKKYGF RDWDSVLAAV GHGGLKEGQV INKLLEIYTK EHKSELTDEK
VLEAAEETKD KLHIRKSKSG IVVKGIHDVS VRFSRCCNPI PGDEIVGYVT RGRGVTIHRT
DCINIINMSL EDRERLIDAE WQSESVGDGE QYTAEINVYA NNRTGLLVDI SKIFTERKID
ITSMNTRTSK QGRATINIAF DIKSKEELGS LVEKIRQVES VLDIGRTTG
//
