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Database: UniProt
Entry: A0A0U3AEL3_9ALTE
LinkDB: A0A0U3AEL3_9ALTE
Original site: A0A0U3AEL3_9ALTE 
ID   A0A0U3AEL3_9ALTE        Unreviewed;       707 AA.
AC   A0A0U3AEL3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=AT746_01815 {ECO:0000313|EMBL:ALS97137.1};
OS   Lacimicrobium alkaliphilum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Lacimicrobium.
OX   NCBI_TaxID=1526571 {ECO:0000313|EMBL:ALS97137.1, ECO:0000313|Proteomes:UP000068447};
RN   [1] {ECO:0000313|EMBL:ALS97137.1, ECO:0000313|Proteomes:UP000068447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YelD216 {ECO:0000313|EMBL:ALS97137.1,
RC   ECO:0000313|Proteomes:UP000068447};
RA   Kim S.-G., Lee Y.-J.;
RT   "Complete genome of Lacimicrobium alkaliphilum KCTC 32984.";
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   -!- 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; CP013650; ALS97137.1; -; Genomic_DNA.
DR   RefSeq; WP_062475638.1; NZ_CP013650.1.
DR   AlphaFoldDB; A0A0U3AEL3; -.
DR   STRING; 1526571.AT746_01815; -.
DR   KEGG; lal:AT746_01815; -.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000068447; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:SF36; 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:ALS97137.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068447}.
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          387..448
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          628..702
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   707 AA;  80181 MW;  385E325162450697 CRC64;
     MYLFEGLKQK VSEYLPAKQV EDIQRAFVLA RDAHDGQMRS SGDPYITHPV AVAGILADMH
     LDYETLMSAL LHDTIEDTPV SKEQLIEEFG QSVADLVEGV SKLDKIQFRS KREAQAENFR
     KMMMAMTQDI RVILVKLADR THNMRTLGAL RPDKRRRIAR ETLEIYAPIA HRLGIHDIKN
     ELEDLGFQAM YPMRYRALGS AVRQARGNRK EIIENTRQEI EIRLKESTID AQVLGREKHL
     YSIYRKMKNK ELLFNEVMDI YAFRLIVEGV DSCYRALGAM HGLYKPIEGR FKDYIAIPRT
     NGYQSLHTSL VGPHGIPVEI QIRTMEMEQM ADKGVAAHWM YKEPGETRGT TAQVRARKWM
     QSLLELQHSA SSSVEFIENV KTDLFPEEIY VFTPDGRIIE LPMGATAVDF AYAVHSDIGN
     SCVGVRVDRR NYSLNRPLQN GQSVEIITSP RAKPNASWLN FVVSAKARSY IRQYLKKQRS
     EEAINMGNRL LRHALGTTKL EEIAEADIDR VVQETKHENF YALLADIGLG NELSAIVARR
     LLGNQEPKII DDGQARVAIK GTEGLLVSYG RCCHPIPGDT IIAILSPGKG MVIHQNGCRN
     IRKLAKEEPH RVLPMNWESK VQGEFKASVR VELINHQGTL AKLTSAIATA DSDIISLQTE
     EKESNIYYID LELTTTNRVH LANVMRKIRA MPEVQKVSRH SQSKQNS
//
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