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Database: UniProt
Entry: E6UIA7_RUMA7
LinkDB: E6UIA7_RUMA7
Original site: E6UIA7_RUMA7 
ID   E6UIA7_RUMA7            Unreviewed;       762 AA.
AC   E6UIA7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE            EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN   OrderedLocusNames=Rumal_1668 {ECO:0000313|EMBL:ADU22168.1};
OS   Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 /
OS   7).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=697329 {ECO:0000313|EMBL:ADU22168.1, ECO:0000313|Proteomes:UP000006919};
RN   [1] {ECO:0000313|EMBL:ADU22168.1, ECO:0000313|Proteomes:UP000006919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7
RC   {ECO:0000313|Proteomes:UP000006919};
RX   PubMed=21914885; DOI=10.1128/JB.05621-11;
RA   Suen G., Stevenson D.M., Bruce D.C., Chertkov O., Copeland A., Cheng J.F.,
RA   Detter C., Detter J.C., Goodwin L.A., Han C.S., Hauser L.J., Ivanova N.N.,
RA   Kyrpides N.C., Land M.L., Lapidus A., Lucas S., Ovchinnikova G.,
RA   Pitluck S., Tapia R., Woyke T., Boyum J., Mead D., Weimer P.J.;
RT   "Complete genome of the cellulolytic ruminal bacterium Ruminococcus albus
RT   7.";
RL   J. Bacteriol. 193:5574-5575(2011).
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; CP002403; ADU22168.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6UIA7; -.
DR   STRING; 697329.Rumal_1668; -.
DR   KEGG; ral:Rumal_1668; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_9; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000006919; 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   Transferase {ECO:0000313|EMBL:ADU22168.1}.
FT   DOMAIN          82..181
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          421..484
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          688..762
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   762 AA;  87069 MW;  7D7E3307707A6BF5 CRC64;
     MSENNRSNGE EAPRRSTYET AEGSLQIPAY ILKASRQVYT IDMIVQKVLD SEKQYDLSKI
     VSAYELAEKY HHDQKRESGE PYISHPIAVG YILLELGMDT DTICAALLHD VVEDTDCTLE
     QLHKMFGIDV TMLVNGVTKL GEVEIFTKDE QKAENIRKIL LAMSEDIRVI IIKLADRLHN
     MRTLNFCRDD KRRTIARETM NIYAPIAHRL GIRSIKDELE DLSFFYLDPF AHEEIEQMMA
     LRRDSREALV ESIKDKIAER LAKEFDPAPT VSGRVKSNYG IYKKVYRDGK DIDEIYDRYA
     VRVIVNTVNE CYNVLGIIHD MFKPIPNRFK DYISTPKANM YQSLHTTVIG REGIPFEVQI
     RTWDMHRLAE YGIAAHWKYK EGVKSNAKDD KRLAWIRQII ENQKESNDVE EIVRAIKSDL
     SPEDVFAFTP KGDMITLPVG STVIDFAYAI HTEVGHRMSG AKVNEKMVSY DHKISTGEII
     EILTSNVAGH GPSRSWLNIA KTNEAKSKIR SWFKKERREE NIFEGRAALE REFRKHMIRV
     PEDELEEFLR LDMKRHNCDT LDDFFAAIGY GGVQLSKLMQ RLKDSYNKKY GEKADESEDS
     VVKPVKSSSG VVVDGIEDCM IKFAQCCNPL PGDEIIGFIT RGHGVSVHKK DCLNYVNQMN
     KGENTERWVN VSWAKNSDRN NTTYFKTTLD IIAVDRIGLL ADVSSALAMI NVFIYESTSR
     ELKNGNALMS ITVSIAGMEQ LKTVMSKLQK IKNVISVERS GK
//
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