ID D3R342_MAGIU Unreviewed; 771 AA.
AC D3R342;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN OrderedLocusNames=HMPREF0868_1337 {ECO:0000313|EMBL:ADC91381.1};
OS Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. BVAB3
OS (strain UPII9-5)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Mageeibacillus.
OX NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC91381.1, ECO:0000313|Proteomes:UP000008234};
RN [1] {ECO:0000313|Proteomes:UP000008234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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; CP001850; ADC91381.1; -; Genomic_DNA.
DR RefSeq; WP_012993018.1; NC_013895.2.
DR AlphaFoldDB; D3R342; -.
DR STRING; 699246.HMPREF0868_1337; -.
DR KEGG; clo:HMPREF0868_1337; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000008234; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008234};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 55..154
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 699..771
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 771 AA; 87925 MW; F236EE08C4F00CC4 CRC64;
MVNASERAAI ENDFKSFLHQ YELYSNTTDN SKLEKAFEYA FQAHIDQRRQ TGEPYITHPL
TVATILLELE VDQATLVAAL LHDTVEDTGT TLEDIADRFG DDVAALVDGV TKLEKIRFSS
KEELQAENFR KMFLAMAKDI RVVLIKLADR LHNMRTLKTM REDKQKRIAQ ETLDIYAPLA
HRLGIYKWKW ELEDLCLRYL DRTAYYELVG AIAQRREERE RYLQEIIIDL QKTVAEMGIN
AEIEGRPKHF YSIYRKMEKK HKSLDQIFDL FACRVIVDTV VDCYTVLGLV HDRFRPIPGR
FKDYIATPKP NMYQSLHTTV FGPKGVPFEI QIRTFEMHRV AEYGIAAHYR YKEGKTGPAR
PGSKESANDT KLAWLRQLLD WQKDMKDAGE FMEGLRNGLI EDEVFVFTPR GDVICLPIGA
TPIDFAYNIH SGIGNRMYGA RINSRIAPID TELKNGDIVE ILTSDKVHGP SRDWLNVVRS
SSARSKINQW FKKEMRDENV QQGKAIFERE LKKTGFTSHQ LMKHEFIDTM LQKNHFNALD
DMFAAIGFGG FSATKAIPKL RDEYIRSLPP DERLKYGYRV NSNGQVVPDQ VTATISEAQV
TSNNKDVKHK RKLNDLGIIV KGMDNCLVHL SRCCNPVVGD AIIGYITRGK GVAVHRRICP
NISKLLSNAC LNSIEAERAS RLIECSWSND ETAGTYTVNV KILARDRSHL LSDITCAIAE
EKVEIVGGSL SAVKDVTATL FFSLEVKDAI QCDRVFGRIK AIRDVMEIHR I
//
