ID K0XTB0_9FIRM Unreviewed; 761 AA.
AC K0XTB0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=HMPREF1135_00633 {ECO:0000313|EMBL:EJZ70864.1};
OS Lachnoanaerobaculum sp. OBRC5-5.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=936595 {ECO:0000313|EMBL:EJZ70864.1, ECO:0000313|Proteomes:UP000006070};
RN [1] {ECO:0000313|EMBL:EJZ70864.1, ECO:0000313|Proteomes:UP000006070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OBRC5-5 {ECO:0000313|EMBL:EJZ70864.1,
RC ECO:0000313|Proteomes:UP000006070};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sizova M., Hazen A.,
RA Epstein S., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridiales bacterium OBRC5-5.";
RL Submitted (JUL-2012) 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:EJZ70864.1}.
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DR EMBL; ALOA01000004; EJZ70864.1; -; Genomic_DNA.
DR RefSeq; WP_007591931.1; NZ_JH815185.1.
DR AlphaFoldDB; K0XTB0; -.
DR STRING; 936595.HMPREF1135_00633; -.
DR PATRIC; fig|1125778.3.peg.638; -.
DR HOGENOM; CLU_012300_3_0_9; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000006070; 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 Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 71..171
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 417..478
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 687..761
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 761 AA; 86963 MW; 7BEB33D19FAE8B8F CRC64;
MKEDKLNFLD ENIETPIDKP ADFTSPESLY KKLVDIILHY HPSDDITMIS KAYELAKKAH
NDQKRKSGEP YIIHPICVAI ILAELELDKE TIAAGLLHDV IEDTAISFEE LSNIFGVDVA
NLVDGVTKLT QLSLKNDKIE MQAENLRKMF LAMAKDIRVI LIKLADRLHN MRTLQYMKPE
KQKEKARETM DIYSPIAQRL GISKIKVELD DLSLKYLHPD VYYDLSEKLA FRKEQRQQFV
DEIIKKFNEH LSDTGMKYQI SGRVKHLFSI YKKMVNQNKT LDQIYDVFAI RIIVEDVAAC
YLALGTAHEI YKPIPGRFKD YIAMPKPNMY QSLHTTLISD TGQPFEVQIR TFEMHKTAEF
GIAAHWKYKE SGSGTSAQGS EDAKMNWLRQ ILEWQKDTSD NAEFLKVIKS DLDLFSDSVY
CFTPNGDVKN LPAGSNPIDF AYSIHSAVGN KMVGARVNGR LVNIDYELKS GDRVEIITSQ
NSKGPSRDWL NIVKSNQAKS KIQQWFKTEL KEDNILRGKD LLEKYCKAKG INWNEINKPQ
FQEKVMKRYA IKDWDSILAS LGHGGLKEGQ VINKMIEEQK KVAKKEISES ALLESLSDNN
NTAIHKKSKN GITVKGIEDI AVRFSKCCNP VPGDEIVGFI TRGRGVSIHR TDCINVMNLP
SDDRTRLIPA EWQEFEDAKL EEKYQTELQI FAHNRQGLIF DLIRIYSENN ITINNMNART
NKQDISTINL VFDIKGREEL NSLIGKLRQI TGVIDIERAT G
//
