DGTP_ECO57
ID DGTP_ECO57 Reviewed; 505 AA.
AC Q8X8Y9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
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};
GN OrderedLocusNames=Z0171, ECs0164;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other
CC canonical NTPs. {ECO:0000255|HAMAP-Rule:MF_00030}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00030};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00030}.
CC -!- SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00030}.
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DR EMBL; AE005174; AAG54464.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33587.1; -; Genomic_DNA.
DR PIR; D85500; D85500.
DR PIR; D90649; D90649.
DR RefSeq; NP_308191.1; NC_002695.1.
DR RefSeq; WP_000057080.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X8Y9; -.
DR SMR; Q8X8Y9; -.
DR STRING; 155864.EDL933_0165; -.
DR EnsemblBacteria; AAG54464; AAG54464; Z0171.
DR EnsemblBacteria; BAB33587; BAB33587; ECs_0164.
DR GeneID; 913819; -.
DR KEGG; ece:Z0171; -.
DR KEGG; ecs:ECs_0164; -.
DR PATRIC; fig|386585.9.peg.264; -.
DR eggNOG; COG0232; Bacteria.
DR HOGENOM; CLU_028163_2_1_6; -.
DR OMA; ICYTIID; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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 InterPro; IPR026875; PHydrolase_assoc_dom.
DR PANTHER; PTHR11373:SF32; PTHR11373:SF32; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF13286; HD_assoc; 1.
DR SMART; SM00471; HDc; 1.
DR TIGRFAMs; TIGR01353; dGTP_triPase; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..505
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT /id="PRO_0000205281"
FT DOMAIN 66..273
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 505 AA; 59323 MW; 7B5459C3B77DD71A CRC64;
MAQIDFRKKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
AAVRTRLTHS MEVQQVGRYI AKEILSRLKE LKLLEAYGLD ELTGPFESIV EMSCLMHDIG
NPPFGHFGEA AINDWFRQRL HPEDAESQPL TDDRCSVAVL RLRDGEEPLN ELRRKIRQDL
CHFEGNAQGI RLVHTLMRMN LTWAQVGGIL KYTRPAWWRG ETPETHHYLM KKPGYYLSEE
AYIARLRKEL NLALYSRFPL TWIMEAADDI SYCVADLEDA VEKRIFTVEQ LYHHLHEAWG
QHEKGSLFSL VVENAWEKSR SNSLSRSTED QFFMYLRVNT LNKLVPYAAQ RFIDNLPAIF
AGTFNHALLE DASECSDLLK LYKNVAVKHV FSHPDVEQLE LQGYRVISGL LEIYRPLLSL
SLSDFTELVE KERVKRSPIE SRLFHKLSTR HRLAYVEAVS KLPSDSPEFP LWEYYYRCRL
LQDYISGMTD LYAWDEYRRL MAVEQ