DGTP_YERP3
ID DGTP_YERP3 Reviewed; 506 AA.
AC A7FM03;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=YpsIP31758_3324;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS49161.1; -; Genomic_DNA.
DR RefSeq; WP_011191765.1; NC_009708.1.
DR AlphaFoldDB; A7FM03; -.
DR SMR; A7FM03; -.
DR EnsemblBacteria; ABS49161; ABS49161; YpsIP31758_3324.
DR GeneID; 66842831; -.
DR KEGG; ypi:YpsIP31758_3324; -.
DR HOGENOM; CLU_028163_2_1_6; -.
DR OMA; ICYTIID; -.
DR Proteomes; UP000002412; 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.
FT CHAIN 1..506
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT /id="PRO_1000057231"
FT DOMAIN 66..274
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 506 AA; 58438 MW; 9304583B5596309E CRC64;
MSGIDFKQKI SFQRPFSKPS SAEDEYEITR VFESDRGRIV NSAAIRRLQQ KTQVFPLERN
AAVRSRLTHS LEVQQVGRYI AKEILNRFKQ DKKITAYGLD KLLDPFESIV EMACLMHDIG
NPPFGHFGES AINDWFTKRM DPNGGSGSEP QSTDQCQVEV LKLCEGETEL NILRSKIRHD
LSQFEGNAQA IRLVHSLLKL NLTYAQVGCI LKYTKPAYWS APIPASHNYL MKKPGFYLAE
ENYVKELRRE LNMEEFDRFP LTYIMEAADD ISYCIADLED AVEKNIFSVE QLYDHMSQEW
GAVTPGDLFD KVVGAAFRQL GREQGRRSSE DQFFMYLRVN TVGKLVPHAA QRFIENLPAV
FSGSFNQALL EDSSAACKLL QIFKRVAVKH VFNHPEVEQL ELQGYRVISG LLDIYSPLLA
MPETAFTQLV ADDRHRKYPI ETRLFHKLSI KHRLAYAESA ERIRNLPSEQ YEIYEYYYRA
RLIQDYISGM TDLYAYDEYR RLMAAE