(data stored in SCRATCH zone)

SWISSPROT: C8U1N0_ECO10

ID   C8U1N0_ECO10            Unreviewed;       505 AA.
AC   C8U1N0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00030};
DE            Short=dGTP triphosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00030};
DE            Short=dGTPase {ECO:0000256|HAMAP-Rule:MF_00030};
DE            EC=3.1.5.1 {ECO:0000256|HAMAP-Rule:MF_00030};
GN   Name=dgt {ECO:0000256|HAMAP-Rule:MF_00030,
GN   ECO:0000313|EMBL:BAI29038.1};
GN   OrderedLocusNames=ECO103_0160 {ECO:0000313|EMBL:BAI29038.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29038.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29038.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other
CC       canonical NTPs. {ECO:0000256|HAMAP-Rule:MF_00030,
CC       ECO:0000256|SAAS:SAAS00859492}.
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;
CC         EC=3.1.5.1; Evidence={ECO:0000256|HAMAP-Rule:MF_00030,
CC         ECO:0000256|SAAS:SAAS01118130};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00030, ECO:0000256|SAAS:SAAS00859496};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00030}.
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00030, ECO:0000256|SAAS:SAAS00859497}.
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DR   EMBL; AP010958; BAI29038.1; -; Genomic_DNA.
DR   RefSeq; WP_000057094.1; NC_013353.1.
DR   SMR; C8U1N0; -.
DR   EnsemblBacteria; BAI29038; BAI29038; ECO103_0160.
DR   KEGG; eoh:ECO103_0160; -.
DR   HOGENOM; HOG000082150; -.
DR   KO; K01129; -.
DR   OMA; HSGEKAI; -.
DR   BioCyc; ECOL585395:ECO103_RS00820-MONOMER; -.
DR   Proteomes; UP000000959; 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   PANTHER; PTHR11373:SF29; PTHR11373:SF29; 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; C8U1N0.
DR   SWISS-2DPAGE; C8U1N0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00030,
KW   ECO:0000256|SAAS:SAAS00078661, ECO:0000313|EMBL:BAI29038.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00030,
KW   ECO:0000256|SAAS:SAAS00859502}.
FT   DOMAIN       66    273       HD. {ECO:0000259|PROSITE:PS51831}.
SQ   SEQUENCE   505 AA;  59381 MW;  DC256383D8BED53F CRC64;
     MAQIDFRKKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
     AAVRTRLTHS MEVQQVGRYI AKEILSRLKE LKLLEAYGLD ELTGPFESIV EMSCLMHDIG
     NPPFGHFGEA AINDWFRQRL YPEDAESQPL TDDRCSVAAL 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 KERVKRFPIE SRLFHKLSTR HRLAYVEAVS KLPSDSPEFP LWEYYYRCRL
     LQDYISGMTD LYAWDEYRRL MAVEQ
//

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