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
//