ID A0A133XDQ7_9RHOO Unreviewed; 717 AA.
AC A0A133XDQ7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:KXB29056.1};
GN ORFNames=AT959_19765 {ECO:0000313|EMBL:KXB29056.1};
OS Dechloromonas denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=281362 {ECO:0000313|EMBL:KXB29056.1, ECO:0000313|Proteomes:UP000070186};
RN [1] {ECO:0000313|EMBL:KXB29056.1, ECO:0000313|Proteomes:UP000070186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-841 {ECO:0000313|EMBL:KXB29056.1,
RC ECO:0000313|Proteomes:UP000070186};
RA Yoon S., Nissen S., Park D., Sanford R.A., Loeffler F.E.;
RT "Nitrous oxide reduction kinetics distinguish bacteria harboring typical
RT versus atypical NosZ.";
RL Submitted (DEC-2015) 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:KXB29056.1}.
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DR EMBL; LODL01000040; KXB29056.1; -; Genomic_DNA.
DR RefSeq; WP_066887273.1; NZ_LODL01000040.1.
DR AlphaFoldDB; A0A133XDQ7; -.
DR STRING; 281362.AT959_19765; -.
DR Proteomes; UP000070186; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase 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:KXB29056.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070186}.
FT DOMAIN 57..156
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 396..457
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 639..714
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 717 AA; 80401 MW; FE5ACE3DF027E8DF CRC64;
MEPAPSSPPP AIEEPAYRVF LDSLDYLSPE QVALVKKAYA FSAHAHAHQK RMSGEPYITH
PLAVAGAVVE WRMDADAIMA ALLHDVLEDT GTTKRELADL FGREVAELVD GLSKLDKMEF
ASYQEAQAEN FRKMLMAMAR DLRVVLIKLA DRQHNLQTMS AMRPDKRRRI ATETLEIYAP
IALRLGLNKL YRELQDLSFR LIHPHRAEVL ARAMRAARGN RKELLTRILD GIKDKLAHAG
LRADVFGREK SLYSTFRKMK DKHLSFSQVL DIYGFRVVVD NVPTCYLALG ALHSLFKPVP
GKFKDYIAIP KANGYQSLHT TLIGPYGTPV EVQIRSQEMH HVAQEGVAAH WLYKDTEESG
ADLQIKTHKW LQSLLEMQSG DSSEFFENVK IDLFPDEVYI FTPKGKIMAM PRGATVVDFA
YAVHTDVGHH CSAARINHDL SPLRTELRNG DMVEIITSPQ ASPNPIWLTY VKTGRARSKI
RHFLRTMQNE ESARLGERLL RQELLSLGVV PISIPTDAWE QLVKSGGQRS IEEVYTDIGL
GKRLPSVVAR RLLAREDMSG DSPGNMALAI HGTEGMAIQL ARCCQPIPGD PIIGSIKKGS
GLVIHTHDCP TIRKSRTAEP QKWIDVEWEP EEGKLFDIRI KVEVKNTRGV LAQVASAIAE
AGSNIEHVSM DADPERLFTL LRFTIQVAHR NHLAAVMRGM RHIPEVTRIV RERGGEA
//
