ID A0A1I1XNS0_9FIRM Unreviewed; 728 AA.
AC A0A1I1XNS0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=SAMN02910327_00310 {ECO:0000313|EMBL:SFE08841.1};
OS Peptostreptococcaceae bacterium pGA-8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=1520829 {ECO:0000313|EMBL:SFE08841.1, ECO:0000313|Proteomes:UP000242361};
RN [1] {ECO:0000313|Proteomes:UP000242361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=pGA-8 {ECO:0000313|Proteomes:UP000242361};
RA Varghese N., Submissions S.;
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 -!- 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; FONK01000002; SFE08841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1XNS0; -.
DR STRING; 1520829.SAMN02910327_00310; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000242361; Unassembled WGS sequence.
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:SFE08841.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242361};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SFE08841.1}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 385..448
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 654..728
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 728 AA; 82620 MW; 159AA09891011B78 CRC64;
MKSREEYLDL LLEINSGYDR LLIGKALDLA TTLHKGQARK SGEPYIVHPM AVAIILAELG
MDDATLISGL LHDVVEDTDY TREELIEGFG EEVALLVDGV TKLGAIKFDS KEEAQAENLR
KMFLAMSKDI RVLIIKLADR LHNMRTIEFM KPEKIIEKSR ETLDIYAPLA SRLGIYAVKF
ELEDLALKYL HPVEYATLHN EIELKKTQRE DFINQVMDEI RESMADMNIN YEIMGRSKHI
YSVYKKMVIQ HKQIGEIFDL TAIRIIVENV RECYAVLGLV HTMWKPIPGR FKDYIAMPKV
NMYQSIHTTV IGDSGEPFEI QIRTYEMHRV AEYGIAAHWK YKEGKTDNKD SKDEMKLAWL
RQTLEWQKDL NDPKEFMETL KMDLFSSQVF VFTPKGEVID LPVDSTPLDF AFKIHTDVGC
KCVGAKVNGK MVTIDHVLSN GDIVEIVTSS NSSGPSVDWL KIAKSSSARN KIKQWLKREN
KEDDVAKGKE ALEKYLKKRN YDPQLVAKAG YITKAMKALN YANAGEMYAQ IGKGGTVMSK
FANLIIKYYT DEMNPEISRE DEIKALNKED KRPKRAKETP GIIVKGADNL MIRVSRCCNP
VPGDNIIGFI TKGRGISVHR ADCSNMVNLP EEEKARFIEV EWEDLKASKS YDADICVIAS
DRKGIFSDIS RTCEDMDVHI AGVNAKTGKD ETLNITLTLS ISSTQQINKI QRTLRNVAGV
LNVYRARS
//
