ID A0A2N0WSR8_9GAMM Unreviewed; 698 AA.
AC A0A2N0WSR8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CW748_05365 {ECO:0000313|EMBL:PKF57950.1};
OS Alteromonadales bacterium alter-6D02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=2058087 {ECO:0000313|EMBL:PKF57950.1, ECO:0000313|Proteomes:UP000233605};
RN [1] {ECO:0000313|EMBL:PKF57950.1, ECO:0000313|Proteomes:UP000233605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alter-6D02 {ECO:0000313|Proteomes:UP000233605};
RX PubMed=27311813; DOI=.1038/ncomms11965;
RA Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT "Microbial interactions lead to rapid micro-scale successions on model
RT marine particles.";
RL Nat. Commun. 7:11965-11965(2016).
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:PKF57950.1}.
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DR EMBL; PIZK01000008; PKF57950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0WSR8; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000233605; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000233605}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 386..447
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 624..698
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 698 AA; 78356 MW; 44DB76D8AED5EE33 CRC64;
MYLIENLVEV VSSYLEPSHV KEIEQAYRVA KAAHEGQFRS SGEPYVTHPV AVCQILADMR
LDHETLIAAL LHDVIEDTPV TQEELAAEFG ETVGELVEGV SKLDKLKFRN QQEAQAENFR
KMMMAMVQDL RVILIKLADR THNMRTLGSL RPDKRRRISR ETLDIYAPIA NRLGIHNIKY
ELEELGFKGL YPNRFRVLSE VVRYAKGNRK EVLQNVEQEI SGRIEEAGIK AEIVGRQKNL
YSIYNKMRSK EIQFEDVMDI YAFRIIVDDI DTCYRCLGAM HTLYKPRPGR FKDYIALPKA
NGYQSLHTSL LGPHGIPVEV QIRTDHMDQM ADKGVAAHWV YKNDDDQGTT AQIRARRWIQ
SLHELQQSAG NSFEFIENVK TDLFPEEIYV FTPDSRLLEL PAGSTAVDFA YAVHTDVGNS
CVGARIDRQA YPLSQPLANG QTVEVITAPG SQPNAAWLNF VVTARARSKI RQVLKSRHTE
ESIKLGRRLL KHAMGDIDLD TLDPAKVEQV VKDTNNESFD SLLSNIGLGN AMSLAIAHQL
SDGNLSNGNS DHKVAIKGAE GMLVTYAKCC RPIPGDPIIA HLSPGKGLVI HIESCANIAG
FEKEKDKYLH VQWDNDGEEE YVTAIRVDMV NHQGILAAVT TAIAQAGANI HSMTTEEKEG
KIYTIDANLS VKDRIHMANV LRKVRVLPDV IKVLRTKH
//
