ID A0A415RBM2_9FIRM Unreviewed; 740 AA.
AC A0A415RBM2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=DWZ54_03565 {ECO:0000313|EMBL:RHM56422.1};
OS Mitsuokella sp. AF33-22.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=2292047 {ECO:0000313|EMBL:RHM56422.1, ECO:0000313|Proteomes:UP000284511};
RN [1] {ECO:0000313|EMBL:RHM56422.1, ECO:0000313|Proteomes:UP000284511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF33-22 {ECO:0000313|EMBL:RHM56422.1,
RC ECO:0000313|Proteomes:UP000284511};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RHM56422.1}.
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DR EMBL; QRQA01000004; RHM56422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A415RBM2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000284511; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:RHM56422.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 52..151
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 394..455
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 660..735
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 740 AA; 84077 MW; 0D04C9506CCF2827 CRC64;
MNDKDKEPVT IDTIIDNVRA YSPKANLDLI RRAYEIAQKA HQGQTRVSGE AYIIHPLHVA
EILTELHLDD VTISAALLHD VVEDTTYTLD QMKELFGEEV AMLIDGVTKL GRLQYKSKEE
AQLESYRKMF LAMAKDIRVI MIKLADRLHN MRTLKYMRED KQKRIARETI EIYAPLANRL
GISSIKWELE DLCLRYLEPE IYYDLVENVK QKRKERQSFI ETSIRQIQEK LEEAHIKADI
SGRAKHFYSI YKKMKRDNKD LSEIYDLSAV RVLVDSVKDC YGVLGVIHAM WKPIPGRFKD
YIAMPKSNGY QSLHTTVMTR GYPLEIQIRT FAMHQVSEYG VAAHWKYKEA GKGAKATGAV
DQKMSWLRQM VSLQQELSDP KEYFEALKVD IFSDEVFVFT PKGDVVDLPK GSIPIDFAYR
IHTEVGHHCV GAKVNGKLVP LEYKLKNGDI VSVITNKANN GPSRDWLNIV ASSETRSKIR
SWFKKEKREE NIERGFELIK EEAKHLGYAP KQLLKEGRLQ QVADKLNIQS EDDLLAALGF
GGLTVRSVMT KLIELYKKDL KEATPPDVSK MLSELKTPQH NGKRSRSSHG VLVEGESGLL
VRLARCCNPI PGDQIVGFIT RGRGVSVHRA DCPNVLRDND LSRLIEVSWD IGLDKDYTVE
IEIVCNDKSG ALAELLAVPS EMKLNIRSVN ANPNRNNKTS TVVMGIDVKS ASQVAQIMTK
MRRLKNVYSV TRAMGRNASN
//
