ID A4CEY0_9GAMM Unreviewed; 701 AA.
AC A4CEY0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=PTD2_16987 {ECO:0000313|EMBL:EAR26655.1};
OS Pseudoalteromonas tunicata D2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR26655.1, ECO:0000313|Proteomes:UP000006201};
RN [1] {ECO:0000313|EMBL:EAR26655.1, ECO:0000313|Proteomes:UP000006201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EAR26655.1,
RC ECO:0000313|Proteomes:UP000006201};
RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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}.
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:EAR26655.1}.
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DR EMBL; AAOH01000010; EAR26655.1; -; Genomic_DNA.
DR RefSeq; WP_009840639.1; NZ_CH959302.1.
DR AlphaFoldDB; A4CEY0; -.
DR STRING; 87626.PTD2_16987; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000006201; Unassembled WGS sequence.
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: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 Hydrolase {ECO:0000313|EMBL:EAR26655.1}.
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..701
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 701 AA; 79418 MW; 9F049687DB310CD1 CRC64;
MYLFEGLKKK ISEYLSPEQV ELVQKAYVVS REAHEGQTRS SGEPYITHPV EVTQILATMK
LDHETLMAAL MHDVIEDTDF SQADLAEIFG ATVAELVEGV SKLDKLSFKD KKEFQAENYR
KMIMAMTQDI RVILIKLADR THNMRTLGSL RPEKRRRIAR ETLEIFAPIA NRLGIHDIKN
ELEDLGFQAL YPMRHRALKN EVAKARGNRK EIIQNIRGEI VARLAESGIK AEVSGREKHL
YSIYKKMLNK ELMFNEVMDI YAFRIGVDSM DTCYRSLGVM HNLYKPIETR FKDYIAVPKT
NGYQSLHTSL VGPHGIPVEI QIRTHEMDHM ADKGVAAHWM YKKSGESSGN TAQQRARQWM
QSLLELQQSA GSSFEFVENV KTELFPEEIY VFTPDGRIIE LPMGATAVDF AYAVHTDVGD
TCVGVRVNRK PHPLSRALDT GQTVEVITSP GAHPNATWLN FVVTGKARLG IRNYLKTQRH
EEALSLGRRL LESALGDHSL DDLPDENVRR VLEENQLKTL IELLVAIGTG SLMSILIAKR
LLHSDSADLN EFTKKTKAAI IGTEGMLVSY SKCCRPVPGD DIVAQVSHGK GLTVHRHECK
NIRGWENDKA KFFIVRWEDA PEKEYIAALR IEIINHQGAL AKLTNVISTT SANIVEISTD
EKESNLYIIN LAITVKDRIH VANIMRKIRV MPDVQKVYRR R
//
