ID S0JDJ6_9FIRM Unreviewed; 778 AA.
AC S0JDJ6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=C805_00766 {ECO:0000313|EMBL:EOT26665.1};
OS Eubacterium sp. 14-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1235790 {ECO:0000313|EMBL:EOT26665.1, ECO:0000313|Proteomes:UP000014176};
RN [1] {ECO:0000313|EMBL:EOT26665.1, ECO:0000313|Proteomes:UP000014176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14-2 {ECO:0000313|EMBL:EOT26665.1,
RC ECO:0000313|Proteomes:UP000014176};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Eubacterium bacterium 14-2.";
RL Submitted (APR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOT26665.1}.
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DR EMBL; ASSS01000005; EOT26665.1; -; Genomic_DNA.
DR AlphaFoldDB; S0JDJ6; -.
DR STRING; 1235790.C805_00766; -.
DR PATRIC; fig|1235790.3.peg.799; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_9; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000014176; Unassembled WGS sequence.
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:UP000014176};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 77..177
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 421..486
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 704..778
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 609..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 88388 MW; 651C1BDC894B12A7 CRC64;
MEDMKMIQLN EQEELAMHTD DHIRPTKEFV SPESLYEELI ASVRRYHPST DISLIEKAYK
IADEAHTGQV RKSGEAYIIH PLCVAIILAE LELDKETIVA GILHDVVEDT VMTEEEISQE
FSEEVALLVD GVTKLGQLSY DADKVEVQAE NLRKMFLAMA KDIRVILIKL ADRLHNMRTL
KYMKPEKQKE KARETMDIYA PIAQRLGISK IKIELDDLSL KYLEPEAYYD LVEKVAVRKS
VREEYVSQLV EEVKSHIKGA GIEASIDGRA KHFFSIYKKM VNQDKTLDQI YDLFAIRIIV
NSVKDCYAAL GVIHEMYKPI PGRFKDYIAM PKPNMYQSLH TTLIGPTGQP FEIQIRTLEM
HRTAEFGIAA HWKYKEVSNG NKVTEKNQEE AKLSWLRQIL EWQKDMSDNR EFMSLLKSDL
DLFSDTVFCF TPSGDVKNLP NGSTPIDFAY SIHSAVGNKM IGAKVNGKLV NIDYVIQNGD
RIEVLTSQNS RGPSRDWLNV VKSTQAKNKI NQWFRSEFKE ENISRGKELL AQYCKTKSIN
WPELNQTSYQ ARIMRKYGFR DWESVLAAVG HGGLKEGQII NKMQEYYKKD HKKALTDEDI
LRNGANDGLG AAASNGNSRE KNGRSRSGSG IVVRGIDDVA VRFSRCCAPV PGDEIVGFVT
RGRGISIHRT DCINVINLSE IERVRLLDAE WQAEEGESGR YMAEIKIYGN NRTGLLVDIT
KILTERQIDI NAIHSNTSKQ GVATITLAFE TKGKEELSSM IDKIRQVESV IDIERTRG
//
