ID   A0A0M4PJD5_9GAMM        Unreviewed;       700 AA.
AC   A0A0M4PJD5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   ORFNames=SP60_00035 {ECO:0000313|EMBL:ALE51787.1};
OS   Candidatus Thioglobus autotrophicus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX   NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE51787.1, ECO:0000313|Proteomes:UP000058020};
RN   [1] {ECO:0000313|EMBL:ALE51787.1, ECO:0000313|Proteomes:UP000058020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF1 {ECO:0000313|EMBL:ALE51787.1,
RC   ECO:0000313|Proteomes:UP000058020};
RX   PubMed=26494660;
RA   Shah V., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT   Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01156-15(2015).
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}.
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DR   EMBL; CP010552; ALE51787.1; -; Genomic_DNA.
DR   RefSeq; WP_053950694.1; NZ_CP010552.1.
DR   AlphaFoldDB; A0A0M4PJD5; -.
DR   STRING; 1705394.SP60_00035; -.
DR   KEGG; tho:SP60_00035; -.
DR   PATRIC; fig|1705394.5.peg.7; -.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000058020; Chromosome.
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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000058020}.
FT   DOMAIN          51..150
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          388..451
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          628..700
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   700 AA;  79240 MW;  F5E3F9B54E271217 CRC64;
     MSKNNSRILI SDLCEVLELY MPKSQVEGVY QAYVVAATAH DGQYRKSGEA YVFHPLSVAM
     ILAELQLDYY CIVAALLHDC IEDTSVTYEE IKYDFGYEIA HIVEGVSKLT GLEFHTTVDK
     QAQNFRKLFL AMSDDMRVMV IKLADRLHNM RTLGSMRRDK QLRIAKETVE IHAPIARRLG
     LNSIRVELDN LCFAIIHPFR HKVLVSQIKK QCGNRAKVIK HIQEQLNNRL VQEGLPEVEI
     GGRRKQPCSI YKKMKNKQLK FTQVLDMYAF RVIVKDVAQC YQALGIIHNL YKPLPGKFKD
     YVALPKSNGY QSLHTILFGP NKIFIEVQIR SEDMHFVSEY GIAAHWHYKS DSDNDSELAN
     NWLGSLLDIQ QNSGTSVEFL EETKNDLFPS EVFVFTPGGD IMQLPYRSTV LDFAYMVHTN
     IGHKTIKAKI DQVSAPISAR LHSGQTVEVI TDEQAKPHPS WLQMAVTAKA KSAIKAYLKS
     QSASELIQLG EYLLSNALDY LTIDMVSISA EKWQTCLDEL GCNSLEELHL GIGLSEILVS
     VVLNKLQYDN DKYAVQNIRI SSTRDKAISF AHCCYPIPGD KVSGILTTSK GLVMHRSDCA
     NLVRLKSKQA QWLSIDWQSD ESESFDVKVA VDVDNQRGTL ASIANMISKL ESNIEHIEVQ
     EKDNSIKSLD LVISVVDSKH LYEITQSLKT LKFIQSVRRI
//