ID A0A178KJT3_9GAMM Unreviewed; 702 AA.
AC A0A178KJT3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=A3K86_08595 {ECO:0000313|EMBL:OAN16983.1};
OS Photobacterium jeanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=858640 {ECO:0000313|EMBL:OAN16983.1, ECO:0000313|Proteomes:UP000078503};
RN [1] {ECO:0000313|EMBL:OAN16983.1, ECO:0000313|Proteomes:UP000078503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-40508 {ECO:0000313|EMBL:OAN16983.1,
RC ECO:0000313|Proteomes:UP000078503};
RA Li Y.;
RT "Photobacterium proteolyticum sp. nov. a protease producing bacterium
RT isolated from ocean sediments of Laizhou Bay.";
RL Submitted (MAR-2016) 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:OAN16983.1}.
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DR EMBL; LVHF01000015; OAN16983.1; -; Genomic_DNA.
DR RefSeq; WP_068330491.1; NZ_PYMD01000006.1.
DR AlphaFoldDB; A0A178KJT3; -.
DR STRING; 858640.A3K86_08595; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000078503; 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:OAN16983.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078503}.
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 628..702
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 702 AA; 79571 MW; 2ED8FA83F21539F9 CRC64;
MYLFDSLKEV ATEYLPEPQI EALRQAYLVA RDAHEGQTRS SGEPYIIHPI AVARILAEMR
LDYETLMAAL LHDVIEDTEV TKEDLETRFS ATVAELVDGV SKLDKLKFRD RKEAQAENFR
KMIMAMAHDI RVILIKLADR THNMRTLGAL RPDKRRRIAR ETLEIFSPLA HRLGIHNIKT
ELEELGFEAL YPNRYKVLKQ VVAAARGNRK EMINKIHAEI EGRLEDAGIE GQVVGREKNL
YSIYNKMKSK EQRFHSIMDI YAFRVLVKDL DTCYRVLGQV HNLYKPRPSR MKDYIAIPKA
NGYQSLHTSL VGPHGVPVEV QIRTEDMDQM ADKGVAAHWT YKNGESSGTT AQVKAQRWMQ
SLLELQQSAG SSFEFIENVK SDLFPDEIYV FTPKGRIVEL PVGATAVDFA YAVHTDVGNA
CVGARVDRQP YPLSKPLKNG QTIDIISAPG ARPNAAWLNY VVTSRARTKI RQVLKTMRRE
ESIILGRRLL NHALGELNID QINPDNLQQV LEDLRLSSMD ELLTDIGLGE LMSVVIARRL
LGNPEELNQH EEETKRRLPI QGADGILLTY ANCCHPIHGD PIVAHVSPGK GLVIHREECS
NIRGYQKEPD KYMAVEWSEE FDQEFVTNLK VDMQNHQGAL ADLTNTIAAT GSNIQGLATE
EKDGRLYTIT VRLTTKGRIH LANIMRRIRV MPNVVRVSRQ KN
//
