ID   K0C7D4_ALCDB            Unreviewed;       701 AA.
AC   K0C7D4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
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   OrderedLocusNames=B5T_00165 {ECO:0000313|EMBL:AFT68453.1};
OS   Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS   B-5) (Alloalcanivorax dieselolei).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alloalcanivorax.
OX   NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT68453.1, ECO:0000313|Proteomes:UP000006286};
RN   [1] {ECO:0000313|EMBL:AFT68453.1, ECO:0000313|Proteomes:UP000006286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC   {ECO:0000313|Proteomes:UP000006286};
RX   PubMed=23144414; DOI=10.1128/JB.01813-12;
RA   Lai Q., Li W., Shao Z.;
RT   "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL   J. Bacteriol. 194:6674-6674(2012).
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; CP003466; AFT68453.1; -; Genomic_DNA.
DR   RefSeq; WP_014992534.1; NC_018691.1.
DR   AlphaFoldDB; K0C7D4; -.
DR   STRING; 930169.B5T_00165; -.
DR   KEGG; adi:B5T_00165; -.
DR   PATRIC; fig|930169.3.peg.164; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000006286; Chromosome.
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:UP000006286}.
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          629..701
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   701 AA;  79070 MW;  4F44B95ADACA6472 CRC64;
     MSTIHNLEKR LRSYLTDEQI APVVRAYYFA ETAHEGQYRR TGDPYITHPL AVANILTDMH
     MDHASLMAAM LHDVIEDTGV SKEQLATEFS EEVAELVDGV SKITQIKFES KAEQQAENLR
     KMILAMTRDI RVVLVKLADR LHNMRTLHVM NPDKRRRIAT ETLEIYAPIA FRLGMYNMRV
     EYEDLAFHAI HPMRARLIGQ AVRSARGNRK EILSSIKTSI EHCLQQEGIE ARVLGREKHL
     YSIYNKMKEQ HKPFSEIMDV FGFRIIVDRV DTCYRVLGAV HNYFIPIPGR FKDYVAIPKA
     NGYQSLHTTL KAHSGIPLEI QIRTEEMEAM ANNGIAAHWL YKTEEKPGSP THTRAQSWMQ
     RLLEMQQKAG NSMEFIENVK VDLFPDEAYV FTPKGDIKEL PAGATPVDFA YAVHTKVGTR
     CVAARVDGKL AALSTPLESG QTVKIITAPN ATPNPAWLNF VVTGKARSNI RHFLKQQRRE
     DARELGQRLL DKALAAYESS LEHLPEAAIR AELDSNDQGN LDELLEDIGM GNRLAPLVAR
     KMMGNHGEAR HEDDRRPLAI SGSEGLIVAY AKCCYPLPGD TILGHLSAGR GIVVHRDTCK
     NLLAEMRNAP EKCIALSWER QAEQEFTAGL RIELVNKRGV LATLANSVTE LGSNIDTIEM
     SDKDPTLSLL NVTLTVKDRI HLARIIKRLR VLDNIVRIHR L
//