DGTP_KLEP3
ID DGTP_KLEP3 Reviewed; 504 AA.
AC B5Y1K9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=KPK_4558;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI10998.1; -; Genomic_DNA.
DR AlphaFoldDB; B5Y1K9; -.
DR SMR; B5Y1K9; -.
DR EnsemblBacteria; ACI10998; ACI10998; KPK_4558.
DR KEGG; kpe:KPK_4558; -.
DR HOGENOM; CLU_028163_2_1_6; -.
DR OMA; ICYTIID; -.
DR OrthoDB; 370035at2; -.
DR Proteomes; UP000001734; 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_1000116919"
FT DOMAIN 66..273
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 504 AA; 59075 MW; 61C1BD1A744EE4C8 CRC64;
MAKIDFRNKI NWRRRFRSPP RVETERDILR IFESDRGRIV NSPAIRRLQQ KTQVFPLERN
AAVRTRLTHS LEVQQVGRYI AKEVLSRLKE QKLLEEYGLE ELTGPFESVV EMACLMHDIG
NPPFGHFGEA AINDWFRQRL APGDALGQPL TDDRCEVQAL RLHEGETALN ALRRKVRQDL
CSFEGNAQGI RLVHTLMRMN LTWAQVGCIL KYTRPAWWFE ATPASHSYLM KKPGYYLAEE
EYVARLRKEL DLAPYNRFPL TWIMEAADDI SYCVADLEDA VEKRIFSAEQ LYQHLYDAWG
NHEKGSLFSQ VVENAWEKSR ANYLRQSAED QFFMYLRVNT LNKLVPYAAR RFIDNLPAIF
TGDFNHALLE DDSDCSQLLE LYKNVAMKQV FSHPDVEQLE LQGYRVISGL LDIYQPLLKL
SLEDFSELVA QERVRRLPIA SRLYQKLSTR HRLAYVEAVN KLVRTAPEFA LMEYYYRCRL
IQDYISGMTD LYAWDEYRRL MAVE