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Protein

Deoxyguanosinetriphosphate triphosphohydrolase

Gene

dgt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.UniRule annotation1 Publication

Catalytic activityi

dGTP + H2O = deoxyguanosine + triphosphate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 Publication

GO - Molecular functioni

  • cobalt ion binding Source: EcoliWiki
  • dGTPase activity Source: EcoCyc
  • GTPase activity Source: EcoliWiki
  • magnesium ion binding Source: UniProtKB-HAMAP
  • manganese ion binding Source: EcoliWiki
  • single-stranded DNA binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciEcoCyc:DGTPTRIPHYDRO-MONOMER.
ECOL316407:JW0156-MONOMER.
MetaCyc:DGTPTRIPHYDRO-MONOMER.
SABIO-RKP15723.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxyguanosinetriphosphate triphosphohydrolaseUniRule annotation (EC:3.1.5.1UniRule annotation)
Short name:
dGTP triphosphohydrolaseUniRule annotation
Short name:
dGTPaseUniRule annotation
Gene namesi
Name:dgtUniRule annotation
Ordered Locus Names:b0160, JW0156
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10225. dgt.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 505504Deoxyguanosinetriphosphate triphosphohydrolasePRO_0000205279Add
BLAST

Proteomic databases

PaxDbiP15723.
PRIDEiP15723.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi4260993. 6 interactions.
DIPiDIP-9437N.
IntActiP15723. 5 interactions.
MINTiMINT-1223226.
STRINGi511145.b0160.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi14 – 174Combined sources
Helixi25 – 4016Combined sources
Helixi43 – 497Combined sources
Beta strandi51 – 555Combined sources
Helixi66 – 9025Combined sources
Helixi95 – 973Combined sources
Helixi103 – 11513Combined sources
Helixi118 – 1203Combined sources
Turni123 – 1253Combined sources
Helixi126 – 14015Combined sources
Helixi142 – 1454Combined sources
Beta strandi146 – 1483Combined sources
Helixi158 – 1603Combined sources
Helixi168 – 18013Combined sources
Helixi185 – 19410Combined sources
Helixi203 – 2097Combined sources
Helixi224 – 2263Combined sources
Turni227 – 2304Combined sources
Beta strandi231 – 2355Combined sources
Helixi240 – 24910Combined sources
Helixi260 – 28223Combined sources
Helixi288 – 29912Combined sources
Helixi307 – 32014Combined sources
Helixi328 – 35427Combined sources
Helixi356 – 3605Combined sources
Beta strandi371 – 3733Combined sources
Helixi374 – 38916Combined sources
Turni390 – 3923Combined sources
Helixi394 – 41926Combined sources
Helixi422 – 43110Combined sources
Helixi438 – 4469Combined sources
Helixi449 – 46012Combined sources
Helixi469 – 48618Combined sources
Helixi490 – 50011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4X9EX-ray3.10A/B/C/D/E/F1-505[»]
4XDSX-ray3.35A/B/C/D/E/F1-505[»]
ProteinModelPortaliP15723.
SMRiP15723. Positions 1-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dGTPase family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C4Q. Bacteria.
COG0232. LUCA.
HOGENOMiHOG000082150.
InParanoidiP15723.
KOiK01129.
OMAiKTDFVHT.
OrthoDBiEOG64XXMV.
PhylomeDBiP15723.

Family and domain databases

Gene3Di1.10.3210.10. 2 hits.
1.10.3410.10. 1 hit.
1.10.3550.10. 2 hits.
HAMAPiMF_00030. dGTPase_type1.
InterProiIPR006261. dGTP_triP_hydro.
IPR023293. dGTP_triP_hydro_central.
IPR020779. dGTP_triP_hydro_proteobacteria.
IPR027432. dGTP_triphosphohydrolase_C_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
[Graphical view]
PfamiPF01966. HD. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01353. dGTP_triPase. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQIDFRKKI NWHRRYRSPQ GVKTEHEILR IFESDRGRII NSPAIRRLQQ
60 70 80 90 100
KTQVFPLERN AAVRTRLTHS MEVQQVGRYI AKEILSRLKE LKLLEAYGLD
110 120 130 140 150
ELTGPFESIV EMSCLMHDIG NPPFGHFGEA AINDWFRQRL HPEDAESQPL
160 170 180 190 200
TDDRCSVAAL RLRDGEEPLN ELRRKIRQDL CHFEGNAQGI RLVHTLMRMN
210 220 230 240 250
LTWAQVGGIL KYTRPAWWRG ETPETHHYLM KKPGYYLSEE AYIARLRKEL
260 270 280 290 300
NLALYSRFPL TWIMEAADDI SYCVADLEDA VEKRIFTVEQ LYHHLHEAWG
310 320 330 340 350
QHEKGSLFSL VVENAWEKSR SNSLSRSTED QFFMYLRVNT LNKLVPYAAQ
360 370 380 390 400
RFIDNLPAIF AGTFNHALLE DASECSDLLK LYKNVAVKHV FSHPDVERLE
410 420 430 440 450
LQGYRVISGL LEIYRPLLSL SLSDFTELVE KERVKRFPIE SRLFHKLSTR
460 470 480 490 500
HRLAYVEAVS KLPSDSPEFP LWEYYYRCRL LQDYISGMTD LYAWDEYRRL

MAVEQ
Length:505
Mass (Da):59,383
Last modified:January 23, 2007 - v4
Checksum:iB04C4CA02AD5B16E
GO

Sequence cautioni

The sequence AAA23716.1 differs from that shown. Reason: Frameshift at positions 90 and 211. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti363 – 3631T → R in AAA23716 (PubMed:2165018).Curated
Sequence conflicti450 – 4501R → P in AAA23716 (PubMed:2165018).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31772 Genomic DNA. Translation: AAA23679.1.
M29955 Genomic DNA. Translation: AAA23716.1. Frameshift.
U70214 Genomic DNA. Translation: AAB08590.1.
U00096 Genomic DNA. Translation: AAC73271.1.
AP009048 Genomic DNA. Translation: BAB96737.1.
PIRiA35993.
RefSeqiNP_414702.1. NC_000913.3.
WP_000057073.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73271; AAC73271; b0160.
BAB96737; BAB96737; BAB96737.
GeneIDi947177.
KEGGiecj:JW0156.
eco:b0160.
PATRICi32115429. VBIEscCol129921_0166.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31772 Genomic DNA. Translation: AAA23679.1.
M29955 Genomic DNA. Translation: AAA23716.1. Frameshift.
U70214 Genomic DNA. Translation: AAB08590.1.
U00096 Genomic DNA. Translation: AAC73271.1.
AP009048 Genomic DNA. Translation: BAB96737.1.
PIRiA35993.
RefSeqiNP_414702.1. NC_000913.3.
WP_000057073.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4X9EX-ray3.10A/B/C/D/E/F1-505[»]
4XDSX-ray3.35A/B/C/D/E/F1-505[»]
ProteinModelPortaliP15723.
SMRiP15723. Positions 1-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260993. 6 interactions.
DIPiDIP-9437N.
IntActiP15723. 5 interactions.
MINTiMINT-1223226.
STRINGi511145.b0160.

Proteomic databases

PaxDbiP15723.
PRIDEiP15723.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73271; AAC73271; b0160.
BAB96737; BAB96737; BAB96737.
GeneIDi947177.
KEGGiecj:JW0156.
eco:b0160.
PATRICi32115429. VBIEscCol129921_0166.

Organism-specific databases

EchoBASEiEB0221.
EcoGeneiEG10225. dgt.

Phylogenomic databases

eggNOGiENOG4105C4Q. Bacteria.
COG0232. LUCA.
HOGENOMiHOG000082150.
InParanoidiP15723.
KOiK01129.
OMAiKTDFVHT.
OrthoDBiEOG64XXMV.
PhylomeDBiP15723.

Enzyme and pathway databases

BioCyciEcoCyc:DGTPTRIPHYDRO-MONOMER.
ECOL316407:JW0156-MONOMER.
MetaCyc:DGTPTRIPHYDRO-MONOMER.
SABIO-RKP15723.

Miscellaneous databases

PROiP15723.

Family and domain databases

Gene3Di1.10.3210.10. 2 hits.
1.10.3410.10. 1 hit.
1.10.3550.10. 2 hits.
HAMAPiMF_00030. dGTPase_type1.
InterProiIPR006261. dGTP_triP_hydro.
IPR023293. dGTP_triP_hydro_central.
IPR020779. dGTP_triP_hydro_proteobacteria.
IPR027432. dGTP_triphosphohydrolase_C_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
[Graphical view]
PfamiPF01966. HD. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01353. dGTP_triPase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli."
    Wurgler S.M., Richardson C.C.
    Proc. Natl. Acad. Sci. U.S.A. 87:2740-2744(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: HR42 and HR44.
  2. "Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli."
    Quirk S., Bhatnagar S.K., Bessman M.J.
    Gene 89:13-18(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
    Fujita N., Mori H., Yura T., Ishihama A.
    Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "The purification and properties of deoxyguanosine triphosphate triphosphohydrolase from Escherichia coli."
    Seto D., Bhatnagar S.K., Bessman M.J.
    J. Biol. Chem. 263:1494-1499(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiDGTP_ECOLI
AccessioniPrimary (citable) accession number: P15723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.