DGTP2_ESCF3
ID DGTP2_ESCF3 Reviewed; 505 AA.
AC Q59435;
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 Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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. {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}.
CC -!- CAUTION: Sequence highly divergent from genome sequence. It could
CC originate from another bacterial species. {ECO:0000305}.
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DR EMBL; U42435; AAA85187.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59435; -.
DR SMR; Q59435; -.
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 3: Inferred from homology;
KW Hydrolase; Magnesium.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..505
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT /id="PRO_0000205282"
FT DOMAIN 66..273
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 505 AA; 59276 MW; 5677CFD72E6C4829 CRC64;
MAQIDFRKKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
AAVRTRLTHS MEVQQVGRYI AKEILSRLKE LKLLEAYGLD ELTGPFESIV EMSCLMHDIG
NPPFGHLGEA AINDWFRQRL HPEDAESQPL TDDRCSVAGL RLRDGEEPLN ELRRKIRQDL
CHFEGNAQGI RLVHTLMRMN LTWAQVGGIL KYTRPAWWRG ETPETHHYLM KKPGYYLSEE
AYIARLRKEL NLALYSRFPL TWIMEAADDI SYCVADLEDA VEKRIFTVEQ LYHHLHEAWG
QHEKGSLFSL VVENAWEKSR SNSLSRSTED QFFMYLRVNT LNKLVPYAAQ RFIDNLPAIF
AGTFNHALLE DASECSDLLK LYKNVAVKHV FSHPDVERLE LQGYRVISGL LEIYRPLLSL
SLSDFTELVE KERVKRFPIE SRLFHKLSTP HRLAYVEAVS KLPSDSPEFP LWEYYYRCRL
LQDYISGMTD LYAWDEYRRL MAVEQ