ID R6T174_9FIRM Unreviewed; 796 AA.
AC R6T174;
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=BN714_00007 {ECO:0000313|EMBL:CDC67213.1};
OS Ruminococcus sp. CAG:57.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262962 {ECO:0000313|EMBL:CDC67213.1, ECO:0000313|Proteomes:UP000018131};
RN [1] {ECO:0000313|EMBL:CDC67213.1, ECO:0000313|Proteomes:UP000018131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:57 {ECO:0000313|Proteomes:UP000018131};
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:CDC67213.1}.
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DR EMBL; CBFS010000207; CDC67213.1; -; Genomic_DNA.
DR AlphaFoldDB; R6T174; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000018131; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000018131}.
FT DOMAIN 115..214
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 454..517
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 722..796
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 19..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 91059 MW; F9246E7B42A86EAD CRC64;
MSDKENILLD PAEMDKIENI PEIKTVSEED LPAESEVKEQ FEEKPAPTAS PDYTDAVPEA
SKPEHIGERS VCSIDALIQK ILDGERQYDL SKIVSAYELA EKYHHNQKRE SGEPYITHPL
SVAYILLELG MDTDTICAAL LHDVVEDTPC TLEELQKNFG SDVAMLVNGV TKLKKVETFT
KDEQKAENIR KILLAMSEDI RVIIIKLADR LHNMRTLNYC KDSKRRTIAH ETMNIYAPIA
HRLGIRSIKD EFEDLAFYYL DPYAYAEIDE QMQLRKGSRE QLVENIKHKI HDRLEKDFDP
VPLIEGRVKS NYGIYKKVYR DGKEIDQIYD RYAVRIIVNT VTECYNVLGI IHDMFRPIPN
RFKDYISTPK ANMYQSLHTT VIGREGIPFE VQIRTWEMHR TAEYGIAAHW KYKEGVRGSS
KDDQRLAWIR QIIESQQESN DVEEIVRAIK NDLAPEDVFA FTPKGDMITL PVGSTVIDFA
YAIHTQVGHK MCGAKVDKKM VSYDYQIKTG EIIEILTTNV EGHGPSRSWL NICKTNEAKS
KIRSWFKKER REENIFEGRN ALEREFRRNN IRVPEEELED FLKMDMHRHS CDTLDDFFAA
IGYGGVQLSK VMQRLKSEYN KKYGEKAQPD TSDLENKIKT SKNSTGVIVD GIDNCAIKFA
QCCNPLPGDE IVGFITRGHG ISVHKKDCVN YLSQKDDPEN AARWINVKWE SSEKHTGYFK
CTLDIVAVDR IGLLADVSSA LAMINIFIYE STSRELKNGN AMLSVTVSIA GMEQLNNVIN
KLQKIKNVIS VERSGK
//