DGTP_YERPE
ID DGTP_YERPE Reviewed; 506 AA.
AC Q8ZBM5; Q0WBR3;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 131.
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=YPO3383, y0806, YP_0302;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL21972.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84393.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60577.1; -; Genomic_DNA.
DR PIR; AI0410; AI0410.
DR RefSeq; WP_002209369.1; NZ_WUCM01000008.1.
DR RefSeq; YP_002348275.1; NC_003143.1.
DR AlphaFoldDB; Q8ZBM5; -.
DR SMR; Q8ZBM5; -.
DR IntAct; Q8ZBM5; 3.
DR STRING; 214092.YPO3383; -.
DR PaxDb; Q8ZBM5; -.
DR DNASU; 1145753; -.
DR EnsemblBacteria; AAM84393; AAM84393; y0806.
DR EnsemblBacteria; AAS60577; AAS60577; YP_0302.
DR GeneID; 57975326; -.
DR KEGG; ype:YPO3383; -.
DR KEGG; ypk:y0806; -.
DR KEGG; ypm:YP_0302; -.
DR PATRIC; fig|214092.21.peg.3864; -.
DR eggNOG; COG0232; Bacteria.
DR HOGENOM; CLU_028163_2_1_6; -.
DR OMA; ICYTIID; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0008832; F:dGTPase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central.
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 CHAIN 1..506
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT /id="PRO_0000205288"
FT DOMAIN 66..274
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 506 AA; 58424 MW; 75BC0E14B179D4CA CRC64;
MSGIDFKQKI SFQRPFSKPS SAEDEYEITR VFESDRGRIV NSAAIRRLQQ KTQVFPLERN
AAVRSRLTHS LEVQQVGRYI AKEILNRFKQ DKKITAYGLD KLLDPFESIV EMACLMHDIG
NPPFGHFGES AINDWFTKRM DPNGGSGSEP QSTDQCQVDV 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
