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Database: UniProt
Entry: A0A0H5LX34_YERIN
LinkDB: A0A0H5LX34_YERIN
Original site: A0A0H5LX34_YERIN 
ID   A0A0H5LX34_YERIN        Unreviewed;       700 AA.
AC   A0A0H5LX34;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   Name=spoT {ECO:0000313|EMBL:CRY55565.1};
GN   ORFNames=ERS008476_02562 {ECO:0000313|EMBL:CRY55565.1};
OS   Yersinia intermedia.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=631 {ECO:0000313|EMBL:CRY55565.1, ECO:0000313|Proteomes:UP000043316};
RN   [1] {ECO:0000313|Proteomes:UP000043316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R148 {ECO:0000313|Proteomes:UP000043316};
RG   Pathogen Informatics;
RL   Submitted (MAR-2015) 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}.
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DR   EMBL; CWJI01000006; CRY55565.1; -; Genomic_DNA.
DR   RefSeq; WP_019213087.1; NZ_CWJI01000006.1.
DR   AlphaFoldDB; A0A0H5LX34; -.
DR   GeneID; 61817729; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000043316; 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:SF36; 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:CRY55565.1}.
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          626..700
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   700 AA;  78930 MW;  DF7CA5B325EA3087 CRC64;
     MYLFESLNLL IQRYLPEEQI KRLKQAYLVA RDAHEGQTRS SGEPYITHPV AVACILAEMR
     LDYETLMAAL LHDVIEDTPA TYQDMEQLFG KSVAELVEGV SKLDKLNFRD KKEAQAENFR
     KMIMAMVQDI RVILIKLADR THNMRTLGSL RPDKRRRIAR ETLEIYSPLA HRLGIHHLKT
     ELEELGFEAL YPNRYRVIKE VVKAARGNRK EMIQKILAEI EGRLTEAGIP CRVSGREKHL
     YSIYCKMNLK EQRFHSIMDI YAFRVIVKEV DTCYRVLGQA HSLYKPRPGR VKDYIAIPKA
     NGYQSLHTSL IGPHGVPVEV QIRTEDMDQM AEMGVAAHWA YKEQGESGTT AQIRAQRWMQ
     SLLELQQSAG SSFEFIESVK SDLFPDEIYV FTPEGRIVEL PAGATPVDFA YAVHTDIGHA
     CVGARVDRQP YPLSQSLSSG QTVEIITAPG ARPNAAWLNF VVSSKARAKI RQLLKNLKRD
     ESVSLGRRLL NHALGNGRKI ADIPEENIKH ELDRMKLATM DDLLAEIGLG NAMSVVVAKN
     LLGDPSTLAA SGARKLPIKG ADGVLITFAK CCRPIPGDPI IAHISPGKGL VIHHESCRNI
     RGYQKEPEKF MAVEWDQETE QEFIAEIKVD MFNQQGALAN LTAAINAAES NIQSLNTEEK
     DGRVYSAFIR LTTRDRVHLA NIMRKIRIMP DVVKVSRNRN
//
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