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DGTP_SHIBO
ID   DGTP_SHIBO              Reviewed;         505 AA.
AC   Q59827;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00030};
DE            Short=dGTP triphosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00030};
DE            Short=dGTPase {ECO:0000255|HAMAP-Rule:MF_00030};
DE            EC=3.1.5.1 {ECO:0000255|HAMAP-Rule:MF_00030};
GN   Name=dgt {ECO:0000255|HAMAP-Rule:MF_00030};
OS   Shigella boydii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, AND
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 9207 / AMC 43-G-58;
RX   PubMed=8995266; DOI=10.1074/jbc.272.1.332;
RA   Quirk S., Do B.T.;
RT   "Cloning, purification, and characterization of the Shigella boydii dGTP
RT   triphosphohydrolase.";
RL   J. Biol. Chem. 272:332-336(1997).
CC   -!- FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other
CC       canonical NTPs.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dGTP + H2O = 2'-deoxyguanosine + H(+) + triphosphate;
CC         Xref=Rhea:RHEA:15193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17172, ChEBI:CHEBI:18036, ChEBI:CHEBI:61429; EC=3.1.5.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00030};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Inhibited by the action of reducing agents such as
CC       dithiothreitol and 2-mercaptoethanol.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.2.;
CC       Temperature dependence:
CC         Thermostable. Fully active at 60 degrees Celsius.;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00030}.
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DR   EMBL; U42434; AAA85188.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59827; -.
DR   SMR; Q59827; -.
DR   GO; GO:0008832; F:dGTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006203; P:dGTP catabolic process; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.3410.10; -; 1.
DR   HAMAP; MF_00030; dGTPase_type1; 1.
DR   InterPro; IPR023293; dGTP_triP_hydro_central_sf.
DR   InterPro; IPR006261; dNTPase.
DR   InterPro; IPR020779; dNTPase_1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   PANTHER; PTHR11373:SF32; PTHR11373:SF32; 1.
DR   Pfam; PF01966; HD; 1.
DR   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR01353; dGTP_triPase; 1.
DR   PROSITE; PS51831; HD; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Magnesium.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..505
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT                   /id="PRO_0000205286"
FT   DOMAIN          66..273
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   505 AA;  59498 MW;  FBA79F1B00613EB2 CRC64;
     MAQIDFRKKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
     AAVRTRLTHS MEVQQVGRYI AKEILSRMKE LKLLEAYGLD ELTGPFESIV EMSCLMHDIG
     NPPFGHFGEA AINDWFRQRL HPEDAESQPL TDDRCRVRGL RLRDGEEPLN ELRRKIRQDL
     CHFEGNAQGI RLVHTLMRMN LTWAQVGGIL KYTRPAWWRG ETPETHHYLM KKPGYYLSEE
     AYIARLRKEL NLALYSRFPL TWIMEAADDI SYCVADLEDA VEKRIYTLEQ LYHHLHDAWG
     QHEKGSLFSL VVENAWEKSR SNSLSRSTED QFFMYLRVNT LNKLVPYAAQ RFIDNLPAIF
     AGTFNHALLE DASECSDLLK LYKNVAVKHV FSHPDVERLE LQGYRVISGL LEIYRPLLSL
     SLSDFTELVE KERVKRFPIE SRLFHKLSTP HRLAYVEAVS KLPSDSPEFP LWEYYYRCRL
     LQDYISGMTD LYAWDEYRRL MAVEQ
 
 
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