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Database: UniProt
Entry: R5NBF5_9FIRM
LinkDB: R5NBF5_9FIRM
Original site: R5NBF5_9FIRM 
ID   R5NBF5_9FIRM            Unreviewed;       716 AA.
AC   R5NBF5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE            EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN   ORFNames=BN804_00966 {ECO:0000313|EMBL:CCY94532.1};
OS   Firmicutes bacterium CAG:884.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262990 {ECO:0000313|EMBL:CCY94532.1, ECO:0000313|Proteomes:UP000018073};
RN   [1] {ECO:0000313|EMBL:CCY94532.1, ECO:0000313|Proteomes:UP000018073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:884 {ECO:0000313|Proteomes:UP000018073};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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:CCY94532.1}.
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DR   EMBL; CAZD010000050; CCY94532.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5NBF5; -.
DR   STRING; 1262990.BN804_00966; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000018073; 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; 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; 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; GTP PYROPHOSPHOKINASE; 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; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018073}.
FT   DOMAIN          49..148
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          392..453
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   716 AA;  82812 MW;  EF657F2A66BB749B CRC64;
     MERTYNTYEE LKELLKTYIK DEDLELIDEC YDFAFKCHQG QRRITGEDYI YHPISVAYIL
     ASINADKETI GAALLHDVLE DCNITREEME EKFGKEITKI VYGVTKINKL NFNDESEVLI
     ANHRKIIVGL AEDVRVIILK LADRLNNLRT LWALPEEKQK KKAKETLEIL TPIADRLGMN
     KMKSEMEDLA LRYLKPDTYF DILEKLNQTK AEREALVLEM QDKITTLLTE NDIKHEIKGR
     AKSIYSIYKK LEKGRRWSDI YDIYALRVFV DTEAECYQVL GIIHSKFRPI PKRFKDYIAM
     PKTNMYQSLH TTVFGVGGNA FEVQIRTYAM DKVAESGIAS HWSYKERGSV KANLQNAMEQ
     KLQFFKTIME LEQENLSKEE FVNTVTNEVF NDTIYVFTPA GDVIELPNGS TPIDFAYKVH
     SNIGNHMVSA IVNGAIRPLN EELKDNDIIK IQTSPSAKPS EEWLKVAKTT QAKQKIKDYF
     KRIAKDGYYK KGQELIAKEL RRKKITNQEF FKDENIEKIL NQLKLNNLDE LYINVGDNKI
     GVNQIINILK EENLSKEELI LKKASDQKVK YSYNDLYVDG VENMKINVAH CCNPVPGDKI
     IGYVTKGNGV TVHRLICPNI EDEEERTIEV KWGNEIKSKY ESMLVLHANE NKSLLMDIIT
     KAQNRDISVT YMNNIFANDL YYIEIKILVK DLDTLNTFIN DVSNLSEVID VERVIQ
//
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