DGTP_CITK8
ID DGTP_CITK8 Reviewed; 504 AA.
AC A8ALC8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=CKO_03207;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000822; ABV14291.1; -; Genomic_DNA.
DR RefSeq; WP_012133997.1; NC_009792.1.
DR AlphaFoldDB; A8ALC8; -.
DR SMR; A8ALC8; -.
DR STRING; 290338.CKO_03207; -.
DR PRIDE; A8ALC8; -.
DR EnsemblBacteria; ABV14291; ABV14291; CKO_03207.
DR GeneID; 45136989; -.
DR KEGG; cko:CKO_03207; -.
DR HOGENOM; CLU_028163_2_1_6; -.
DR OMA; ICYTIID; -.
DR OrthoDB; 370035at2; -.
DR Proteomes; UP000008148; 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; Reference proteome.
FT CHAIN 1..504
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT /id="PRO_1000006545"
FT DOMAIN 66..273
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 504 AA; 59299 MW; 8C83DCAE69344B89 CRC64;
MAQIDFRNKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
AAVRTRLTHS MEVQQVGRYI AKEILSRLKE LKLLEQYGLD ELTGPFESIV EMSCLMHDIG
NPPFGHFGEA AINDWFRQRL HPADAESQPL SDDRCAVAAL RLREGEESLN DIRRKVRQDL
CHFEGNAQGI RLVHTLMRMN LTWAQVGGIL KYTRPAWWRG ETPATHRYLM KKPGYYLSEA
PYIERLRKEL ALAPYSRFPL TWIMEAADDI SYCVADLEDA VEKRIFSVEQ LYHHLYEAWG
HHEKGSLFTQ VVENAWEKSR SNSLSRSTED QFFMYLRVNT LNKLVPYAAQ RFIDNLPQIF
DGSFNHALLE DASSFSQLLE LYKNVAIKHV FSHPDVEQLE LQGYRVISGL LEIYQPLLRM
SLVDFRELVE KERVKRFPIE SRLFQKLSTR HRLAYVEAVS KLSPEAPEYP TLEYYYRCRL
IQDYISGMTD LYAWDEYRRL MAVE