DGTP_CROS8
ID DGTP_CROS8 Reviewed; 504 AA.
AC A7MGS4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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}; OrderedLocusNames=ESA_03180;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU78402.1; -; Genomic_DNA.
DR RefSeq; WP_012125718.1; NC_009778.1.
DR AlphaFoldDB; A7MGS4; -.
DR SMR; A7MGS4; -.
DR EnsemblBacteria; ABU78402; ABU78402; ESA_03180.
DR KEGG; esa:ESA_03180; -.
DR PATRIC; fig|290339.8.peg.2811; -.
DR HOGENOM; CLU_028163_2_1_6; -.
DR OMA; ICYTIID; -.
DR OrthoDB; 370035at2; -.
DR Proteomes; UP000000260; 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..504
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT /id="PRO_1000116918"
FT DOMAIN 66..273
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 504 AA; 58738 MW; CDF3B81FB3DE585C CRC64;
MEKIDFRNKI NWHRRYRSPQ GVKSEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
AAVRTRLTHS LEVQQVGRYI AKEVLSRLKE QGLLEAYGLS ELTGPFESIV EMSCLMHDIG
NPPFGHFGEA AINDWFSQRL FPADAENLPV SQDRCTVQTL RLQEGEEALN ALRGNVRRDL
CHFEGNAQGI RLVHTLLRMN LTWAQVGGIL KYSRPAWHHG PVPETHSYLM KKPGFYLSED
QYISRLRKEL QLDTYSRFPL AWIMEAADDI SYCVADLEDA VEKRIFSVEQ LYQHLYDAWG
EHAPGDLFNL VVQNAWDKSG TNQLHHSAED QFFMYLRVNT LNRLAPYAAQ RFIDNLPDVF
NGSFNHALLE DDSPYSRLLE LYKNVAVRHV FNHPDVEQLE LQGYRVISGL LDIYSPLLAL
TLAQFRELVE KESVRSLPIE SRLYHKLSSR HRLAYIEAVS HLHPQAADFP VWEYYYRCRL
IQDYISGMTD LYAWDEYRKL MAVE