GenomeNet

Database: UniProt
Entry: I4WFQ6_9GAMM
LinkDB: I4WFQ6_9GAMM
Original site: I4WFQ6_9GAMM 
ID   I4WFQ6_9GAMM            Unreviewed;       720 AA.
AC   I4WFQ6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=UU5_03852 {ECO:0000313|EMBL:EIL98297.1};
OS   Rhodanobacter sp. 115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL98297.1, ECO:0000313|Proteomes:UP000004557};
RN   [1] {ECO:0000313|EMBL:EIL98297.1, ECO:0000313|Proteomes:UP000004557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=115 {ECO:0000313|EMBL:EIL98297.1,
RC   ECO:0000313|Proteomes:UP000004557};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(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}.
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:EIL98297.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJXS01000102; EIL98297.1; -; Genomic_DNA.
DR   RefSeq; WP_008209493.1; NZ_AJXS01000102.1.
DR   AlphaFoldDB; I4WFQ6; -.
DR   PATRIC; fig|1162282.3.peg.739; -.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000004557; 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;
FT   DOMAIN          58..157
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          399..460
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          646..717
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   720 AA;  79656 MW;  0E2ADB8F7E1D3916 CRC64;
     MPAATHPPLD PSVLPPYVLA LRERLGYLPE SQIERVLRAY EVGAHAHEGQ ARKSGEPYIT
     HPVAVAGILA ELGMDAETII AAILHDTLED TELSRSALAS EFGETVAELV DGVTKLDKMK
     FGSRQEADAE SFRKMLLAMA RDLRVILIKL SDRLHNMRTL GAKDAPSRRR IARETLEIYA
     PIAQRLGMNK IKAELQDLGF RALYPDRYRV ISERIRAALG NRREAMGKIE EALSARLAAD
     QLPARVVGRI KSPWSIYSKM HSEHKSFAQL MDVYGFRVVV DSAMSCYMAL GVVHALYKPV
     DRRFKDFIAI PKANGYQSLH TVLLGPFGAP IEVQIRTAEM DSVAESGVAA HWAYKTDSGP
     ANSAQARARE WLSSLADSSV HTASSAEFIE NVKIDLFPDE VYLFTPRGDI LALPRNATAL
     DFAYAVHTDV GDHAVAARVD KKLLPLRTRL ESGQLVEIIT APSAVPNPAW LEVVVTGKAR
     TAIRQYLKHL QHEDAVDFGH RMLDRALDAL GSSLEVIPPT VLDRFLHESK FKRLEELLSD
     IALGNRMPDQ VASQLVATRG RRSHEASALV HPAEKIRITG AERGVLSFAN CCHPLPGDEI
     IGYLSSGKGI VVHRAECPNV VELRKSPERC VGIEWDRDVQ GDYRAELRIE VINRPGVLAT
     IAAAIAAADS NIENVEYVER DLAAATLLFT IEVRNRKHLA DVMRRVRRTG VVSGVYRYPL
//
DBGET integrated database retrieval system