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Database: UniProt
Entry: F7RXP5_9GAMM
LinkDB: F7RXP5_9GAMM
Original site: F7RXP5_9GAMM 
ID   F7RXP5_9GAMM            Unreviewed;       704 AA.
AC   F7RXP5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=A28LD_1024 {ECO:0000313|EMBL:EGN75411.1};
OS   Idiomarina sp. A28L.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN75411.1, ECO:0000313|Proteomes:UP000053031};
RN   [1] {ECO:0000313|EMBL:EGN75411.1, ECO:0000313|Proteomes:UP000053031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A28L {ECO:0000313|EMBL:EGN75411.1,
RC   ECO:0000313|Proteomes:UP000053031};
RX   PubMed=21742887; DOI=10.1128/JB.05648-11;
RA   Gupta H.K., Singh A., Sharma R.;
RT   "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong Lake,
RT   India.";
RL   J. Bacteriol. 193:5875-5876(2011).
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:EGN75411.1}.
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DR   EMBL; AFPO01000012; EGN75411.1; -; Genomic_DNA.
DR   RefSeq; WP_007420001.1; NZ_AFPO01000012.1.
DR   AlphaFoldDB; F7RXP5; -.
DR   STRING; 1036674.A28LD_1024; -.
DR   PATRIC; fig|1036674.4.peg.1016; -.
DR   eggNOG; COG0317; Bacteria.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000053031; 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:UP000053031}.
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          630..704
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   704 AA;  80096 MW;  CD990FC8CA69584E CRC64;
     MYLFEGLRTL TEAYLPADQV TRLEQAFVVA FDAHGEQKRQ SGEPYITHPV AVACMLAEMR
     LDHETLMAAL LHDVIEDTPV TQEDLAEQFG PTVAELVEGV SKLDKLQFNS KEEHQIENYR
     KMIMAMVQDI RVILIKLADR THNMRTIGSL RPDKRRRIGR ETLEIYAPLA HRLGIHNIKN
     ELETLGFHAL YPWRARLLDS QVRKARGNRK ALLVRTHDEV LSRLGEMGIR ARVYGREKHL
     YSIYKKMLNK ELKFTQVMDI YAFRVVVDSV DTCYRVLGAV HNLYKPIETR FKDYIAIPKS
     NGYQSLHTSL KGPHGVPLEI QIRTEEMDLM ADRGVAAHWL YKDIEDSGTT AQVRAQKWMQ
     SLIELQQSAG NSFEFIENVK SDLFPDEIYV FTPDGRIIEL PQGATPVDFA YAVHTDIGTT
     CIGARVNHKA YSLSKPLETG QTVEIRTAPG SRPNIAWLNF VVTGKARLKI RQYLKNQEFD
     EALVLGERLL RASLGNINMN DIKEAEFTRV AHELKREDKQ SLLRDIGLGN LMGVAVVRRL
     IGDEQRLKAA AGDDERGRSL AIKGADGLLL SFAKCCRPIP GDDIIAHVSP GRGLVIHRRE
     CKNVRGHEEE PGRYFAVQWD NKPDSQFVSE IRVEVVNHQG ALAQLTQQIA RTGCNIHGLK
     TEEIDSSIYY IDVALTINDR KHLADVMRQI RKMPHVQRVS RLRK
//
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