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
//