ID R6QYH5_9BACT Unreviewed; 762 AA.
AC R6QYH5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Guanosine-3' 5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:CDC27022.1};
GN ORFNames=BN637_00254 {ECO:0000313|EMBL:CDC27022.1};
OS Prevotella sp. CAG:386.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262925 {ECO:0000313|EMBL:CDC27022.1, ECO:0000313|Proteomes:UP000018046};
RN [1] {ECO:0000313|EMBL:CDC27022.1, ECO:0000313|Proteomes:UP000018046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:386 {ECO:0000313|Proteomes:UP000018046};
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 -!- 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:CDC27022.1}.
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DR EMBL; CBEZ010000178; CDC27022.1; -; Genomic_DNA.
DR AlphaFoldDB; R6QYH5; -.
DR STRING; 1262925.BN637_00254; -.
DR Proteomes; UP000018046; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; 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:CDC27022.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018046}.
FT DOMAIN 64..164
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 414..475
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 689..762
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 762 AA; 87290 MW; 067BEC7E5661D3C5 CRC64;
MDDQNLKDLE REQADNKLIG DAFQHLLDTY VASRHRKKVD IVTKAFNFAR QAHKGVRRLS
GEPYIMHPIA VAQIACEEMG LGSTSICAAL LHDVVEDTDY TVEDISNIFG EKIAQIVDGL
TKISGGIFGD KASAQAENFK KLLLTMSDDI RVILIKICDR LHNMRTLASQ PANKQYKIAG
ETLYIYAPLA NRLGLNKIKT ELEDLSFRYD HPQEYANIEH KLADTEAQRD TLFSQFTQPI
REELDKMGIQ YKIKARVKSP YSIWNKMQNK HVSFDEIYDI LAVRIIFTPK ERANEVNECF
NIYVAISQIY KSHPDRLRDW LNHPKANGYQ ALHVTLMSKQ GRWIEVQIRS DRMDEVAEQG
FAAHWKYKEG EDAEYTEDEN ELNDWLGTIK EILDDPQPDA MDFLDAIKLN LFASEIFVFT
PKGEIKTMPA GCTALDFAFQ IHTFLGSHCI GAKVNHKLVP LSHKLQSGDQ VEILTSKSQH
VQPSWINFVS TAKAKSKIQA ILRRDNREIQ KKGEDILNEW LKKNSLEVNN SILDKLCDYH
HIQKHENFFQ ALGDHCILLG EKDLDELQGK NKKDKSSSSW RNYIPFLGKS KDKKADEKDN
KPQQLMVVGK DFNKKKPLII TEENISQFIF PSCCHAIPGD DIMGYIDNKN RIEIHKRSCS
VAAKLKSSYG NRIVDAKWQM HKLMYFDATI EIKGIDRKGM LLDVSRVISD QLNVNIHKLT
ISSDNGIFDG CIEIRIHDRE DVKVIMDNLK TIDGLQDVQR IL
//
