(data stored in ACNUC7421 zone)

SWISSPROT: DGTP_ECODH

ID   DGTP_ECODH              Reviewed;         505 AA.
AC   B1XD30;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 63.
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=ECDH10B_0140;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other
CC       canonical NTPs. {ECO:0000255|HAMAP-Rule:MF_00030}.
CC   -!- CATALYTIC ACTIVITY: dGTP + H(2)O = deoxyguanosine + triphosphate.
CC       {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}.
DR   EMBL; CP000948; ACB01339.1; -; Genomic_DNA.
DR   RefSeq; WP_000057073.1; NC_010473.1.
DR   ProteinModelPortal; B1XD30; -.
DR   SMR; B1XD30; -.
DR   EnsemblBacteria; ACB01339; ACB01339; ECDH10B_0140.
DR   KEGG; ecd:ECDH10B_0140; -.
DR   eggNOG; ENOG4105C4Q; Bacteria.
DR   eggNOG; COG0232; LUCA.
DR   HOGENOM; HOG000082150; -.
DR   KO; K01129; -.
DR   OMA; FVHNRLT; -.
DR   GO; GO:0008832; F:dGTPase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006203; P:dGTP catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.3410.10; -; 1.
DR   HAMAP; MF_00030; dGTPase_type1; 1.
DR   InterPro; IPR023293; dGTP_triP_hydro_central.
DR   InterPro; IPR006261; dNTPase.
DR   InterPro; IPR020779; dNTPase_1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   PANTHER; PTHR11373:SF34; PTHR11373:SF34; 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;
DR   PRODOM; B1XD30.
DR   SWISS-2DPAGE; B1XD30.
KW   Hydrolase; Magnesium.
FT   CHAIN         1    505       Deoxyguanosinetriphosphate
FT                                triphosphohydrolase.
FT                                /FTId=PRO_1000090260.
FT   DOMAIN       66    273       HD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01175}.
SQ   SEQUENCE   505 AA;  59383 MW;  B04C4CA02AD5B16E CRC64;
     MAQIDFRKKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
     AAVRTRLTHS MEVQQVGRYI AKEILSRLKE LKLLEAYGLD ELTGPFESIV EMSCLMHDIG
     NPPFGHFGEA AINDWFRQRL HPEDAESQPL TDDRCSVAAL 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 SRLFHKLSTR HRLAYVEAVS KLPSDSPEFP LWEYYYRCRL
     LQDYISGMTD LYAWDEYRRL MAVEQ
//

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