DGTP_ECOLI
ID DGTP_ECOLI Reviewed; 505 AA.
AC P15723;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 190.
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=b0160, JW0156;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HR42, and HR44;
RX PubMed=2157212; DOI=10.1073/pnas.87.7.2740;
RA Wurgler S.M., Richardson C.C.;
RT "Structure and regulation of the gene for dGTP triphosphohydrolase from
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2740-2744(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2165018; DOI=10.1016/0378-1119(90)90200-b;
RA Quirk S., Bhatnagar S.K., Bessman M.J.;
RT "Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-
RT encoding gene (dgt) of Escherichia coli.";
RL Gene 89:13-18(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBUNIT.
RX PubMed=2826481; DOI=10.1016/s0021-9258(19)57330-6;
RA Seto D., Bhatnagar S.K., Bessman M.J.;
RT "The purification and properties of deoxyguanosine triphosphate
RT triphosphohydrolase from Escherichia coli.";
RL J. Biol. Chem. 263:1494-1499(1988).
CC -!- FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other
CC canonical NTPs. {ECO:0000255|HAMAP-Rule:MF_00030,
CC ECO:0000269|PubMed:2826481}.
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 ECO:0000269|PubMed:2826481};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00030,
CC ECO:0000269|PubMed:2826481};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00030,
CC ECO:0000269|PubMed:2826481}.
CC -!- SIMILARITY: Belongs to the dGTPase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00030}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23716.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M31772; AAA23679.1; -; Genomic_DNA.
DR EMBL; M29955; AAA23716.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U70214; AAB08590.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73271.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96737.1; -; Genomic_DNA.
DR PIR; A35993; A35993.
DR RefSeq; NP_414702.1; NC_000913.3.
DR RefSeq; WP_000057073.1; NZ_LN832404.1.
DR PDB; 4X9E; X-ray; 3.10 A; A/B/C/D/E/F=1-505.
DR PDB; 4XDS; X-ray; 3.35 A; A/B/C/D/E/F=1-505.
DR PDB; 6OI7; X-ray; 2.90 A; A/B/C/D/E/F=1-505.
DR PDB; 6OIV; X-ray; 3.06 A; A/B/C/D/E/F=1-505.
DR PDB; 6OIW; X-ray; 3.35 A; A/B/C/D/E/F=1-505.
DR PDB; 6OIX; X-ray; 3.15 A; A/B/C/D/E/F=1-505.
DR PDB; 6OIY; X-ray; 3.29 A; A/B/C/D/E/F=1-505.
DR PDBsum; 4X9E; -.
DR PDBsum; 4XDS; -.
DR PDBsum; 6OI7; -.
DR PDBsum; 6OIV; -.
DR PDBsum; 6OIW; -.
DR PDBsum; 6OIX; -.
DR PDBsum; 6OIY; -.
DR AlphaFoldDB; P15723; -.
DR SMR; P15723; -.
DR BioGRID; 4260993; 6.
DR DIP; DIP-9437N; -.
DR IntAct; P15723; 5.
DR STRING; 511145.b0160; -.
DR jPOST; P15723; -.
DR PaxDb; P15723; -.
DR PRIDE; P15723; -.
DR EnsemblBacteria; AAC73271; AAC73271; b0160.
DR EnsemblBacteria; BAB96737; BAB96737; BAB96737.
DR GeneID; 947177; -.
DR KEGG; ecj:JW0156; -.
DR KEGG; eco:b0160; -.
DR PATRIC; fig|1411691.4.peg.2120; -.
DR EchoBASE; EB0221; -.
DR eggNOG; COG0232; Bacteria.
DR HOGENOM; CLU_028163_2_1_6; -.
DR InParanoid; P15723; -.
DR OMA; ICYTIID; -.
DR PhylomeDB; P15723; -.
DR BioCyc; EcoCyc:DGTPTRIPHYDRO-MON; -.
DR BioCyc; MetaCyc:DGTPTRIPHYDRO-MON; -.
DR BRENDA; 3.1.5.1; 2026.
DR SABIO-RK; P15723; -.
DR PRO; PR:P15723; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IDA:EcoliWiki.
DR GO; GO:0008832; F:dGTPase activity; IDA:EcoCyc.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoliWiki.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IDA:EcoliWiki.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc.
DR GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Magnesium;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2826481"
FT CHAIN 2..505
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase"
FT /id="PRO_0000205279"
FT DOMAIN 66..273
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT CONFLICT 363
FT /note="T -> R (in Ref. 2; AAA23716)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="R -> P (in Ref. 2; AAA23716)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6OI7"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:6OI7"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 66..90
FT /evidence="ECO:0007829|PDB:6OI7"
FT TURN 94..98
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:6OI7"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:6OI7"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:6OI7"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6OI7"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:6OIX"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:6OI7"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6OIV"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6OI7"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:6OI7"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:6OI7"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6OIY"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6OIY"
FT HELIX 307..318
FT /evidence="ECO:0007829|PDB:6OI7"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6OIY"
FT HELIX 328..354
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 356..361
FT /evidence="ECO:0007829|PDB:6OI7"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 374..389
FT /evidence="ECO:0007829|PDB:6OI7"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 394..418
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 422..430
FT /evidence="ECO:0007829|PDB:6OI7"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:6OIV"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 449..460
FT /evidence="ECO:0007829|PDB:6OI7"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:6OIY"
FT HELIX 469..486
FT /evidence="ECO:0007829|PDB:6OI7"
FT HELIX 490..500
FT /evidence="ECO:0007829|PDB:6OI7"
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
