ID V5BP24_9GAMM Unreviewed; 722 AA.
AC V5BP24;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=guanosine-3',5'-bis(diphosphate) 3'-diphosphatase {ECO:0000256|ARBA:ARBA00024387};
DE EC=3.1.7.2 {ECO:0000256|ARBA:ARBA00024387};
GN Name=spoT {ECO:0000313|EMBL:ESS67927.1};
GN ORFNames=MGMO_155c00070 {ECO:0000313|EMBL:ESS67927.1};
OS Methyloglobulus morosus KoM1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methyloglobulus.
OX NCBI_TaxID=1116472 {ECO:0000313|EMBL:ESS67927.1, ECO:0000313|Proteomes:UP000017842};
RN [1] {ECO:0000313|EMBL:ESS67927.1, ECO:0000313|Proteomes:UP000017842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KoM1 {ECO:0000313|EMBL:ESS67927.1,
RC ECO:0000313|Proteomes:UP000017842};
RX PubMed=24356841;
RA Poehlein A., Deutzmann J.S., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of the Methanotrophic Gammaproteobacterium
RT Methyloglobulus morosus DSM 22980 Strain KoM1.";
RL Genome Announc. 1:e01078-13(2013).
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=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC Evidence={ECO:0000256|ARBA:ARBA00024273};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC 1/1. {ECO:0000256|ARBA:ARBA00024329}.
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:ESS67927.1}.
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DR EMBL; AYLO01000142; ESS67927.1; -; Genomic_DNA.
DR RefSeq; WP_023496296.1; NZ_AYLO01000142.1.
DR AlphaFoldDB; V5BP24; -.
DR STRING; 1116472.MGMO_155c00070; -.
DR PATRIC; fig|1116472.3.peg.3685; -.
DR eggNOG; COG0317; Bacteria.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000017842; Unassembled WGS sequence.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase 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 Hydrolase {ECO:0000313|EMBL:ESS67927.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017842}.
FT DOMAIN 59..158
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 398..461
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 648..722
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 722 AA; 81661 MW; E97DAC4CB40B5588 CRC64;
MLDVADSIEL ERPQDKLVRR LCSTLSGYLD KDQVDACVRA YEFGAKAHSG QFRKSGEAYI
CHPVAVAISL AEIRMDANCI VAAILHDVIE DTGVSKQELA KAFNPEVAEL VDAVTKLTKI
DSKSHAETQA ENVRKMFLAM GKDLRVIMVK LADRLHNMQT LGAMPAEAKR RIARETLDIY
APIANRLGMN NIRHKLELLS FHAMYPRRYN ILDNALKKAR GNRRKIIDVI ESTLKNRISQ
AKLVCEVSGR EKNLYSIYQK MLHKKVSLND VFDVYAFRIF CDSVDDCYRI LGIVHNLYKP
IPGKFKDYIA LPKANGYQSL HTILIGPFGF PIEIQIRTHE MHRMAESGIA AHWLYKSDDD
KNDKFQDRAN EWLRDLLEIQ QTAGDSLEFI DNLKIDLFPQ EVFVFTPKGE IIKMPRGASI
IDFAYAVHTD IGNACVSARV DRKLVPLQTQ LENGVTVEVI TAIWARPNPL WLNYVTTAKA
RSGIRNYLKN FKQQEAISLG RRLLDKEFQA MHLQLDAIDQ SKIKALLKIS GKKTLDELLE
DIGLGNKMPF LIAKQLTQDD IHAAIRLDDK EQNQRAPLVI KGTEGMVITL AKCCRPIPGD
SIIGFFNPGK GIVVHHHDCR NSNDVRKKQT SWLDVEWSQD TTGEFPAELR LEILNQRGSL
ATVATTISEN NSNIENVTVI EQDSRVSVDL ITISVKDRVH LAQIMRKLKD LPIVIKITRV
KA
//
