Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P04547

- GSTB_BPT4

UniProt

P04547 - GSTB_BPT4

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA beta-glucosyltransferase

Gene

bgt

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA. Is involved in a DNA modification process to protect the phage genome against its own nucleases and the host restriction endonuclease system.1 Publication

Catalytic activityi

Transfers a beta-D-glucosyl residue from UDP-glucose to an hydroxymethylcytosine residue in DNA.

Pathwayi

GO - Molecular functioni

  1. DNA beta-glucosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA modification Source: UniProtKB-UniPathway
  2. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Host-virus interaction, Restriction-modification system evasion by virus

Enzyme and pathway databases

UniPathwayiUPA00198.

Protein family/group databases

CAZyiGT63. Glycosyltransferase Family 63.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA beta-glucosyltransferase (EC:2.4.1.27)
Short name:
BGT
Short name:
Beta-GT
Gene namesi
Name:bgt
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
ProteomesiUP000009087: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351DNA beta-glucosyltransferasePRO_0000164942Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108
Beta strandi14 – 174
Helixi18 – 3215
Beta strandi37 – 437
Beta strandi46 – 505
Helixi51 – 533
Helixi56 – 583
Beta strandi60 – 656
Beta strandi73 – 753
Helixi78 – 8912
Beta strandi94 – 985
Helixi109 – 1124
Helixi118 – 1203
Helixi123 – 1264
Beta strandi132 – 1376
Helixi142 – 1476
Turni148 – 1503
Beta strandi152 – 1598
Helixi162 – 1643
Helixi165 – 1684
Beta strandi169 – 1713
Beta strandi182 – 1876
Helixi191 – 1933
Helixi196 – 2038
Beta strandi210 – 2156
Helixi218 – 2203
Beta strandi233 – 2353
Helixi240 – 2423
Helixi243 – 2475
Beta strandi250 – 2556
Helixi259 – 2613
Turni262 – 2643
Helixi268 – 2747
Beta strandi276 – 2838
Helixi284 – 2863
Helixi296 – 2983
Beta strandi299 – 3024
Helixi303 – 31513
Helixi317 – 33519
Helixi338 – 34811

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BGTX-ray2.20A1-351[»]
1BGUX-ray2.20A1-351[»]
1C3JX-ray1.88A1-351[»]
1IXYX-ray2.50A/B1-351[»]
1J39X-ray1.87A1-351[»]
1JEJX-ray2.50A1-351[»]
1JG6X-ray1.90A1-351[»]
1JG7X-ray1.65A1-351[»]
1JIUX-ray2.50A1-351[»]
1JIVX-ray2.07A1-351[»]
1JIXX-ray1.65A1-351[»]
1M5RX-ray1.80A/B1-351[»]
1NVKX-ray1.80A1-351[»]
1NZDX-ray2.00A1-351[»]
1NZFX-ray2.10A1-351[»]
1QKJX-ray2.30A1-351[»]
1SXPX-ray2.50A/B1-351[»]
1SXQX-ray1.80A/B1-351[»]
2BGTX-ray2.20A1-351[»]
2BGUX-ray2.20A1-351[»]
ProteinModelPortaliP04547.
SMRiP04547. Positions 1-351.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04547.

Family & Domainsi

Family and domain databases

InterProiIPR015281. Phage_T4_Bgt.
[Graphical view]
PfamiPF09198. T4-Gluco-transf. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04547-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIAIINMGN NVINFKTVPS SETIYLFKVI SEMGLNVDII SLKNGVYTKS
60 70 80 90 100
FDEVDVNDYD RLIVVNSSIN FFGGKPNLAI LSAQKFMAKY KSKIYYLFTD
110 120 130 140 150
IRLPFSQSWP NVKNRPWAYL YTEEELLIKS PIKVISQGIN LDIAKAAHKK
160 170 180 190 200
VDNVIEFEYF PIEQYKIHMN DFQLSKPTKK TLDVIYGGSF RSGQRESKMV
210 220 230 240 250
EFLFDTGLNI EFFGNAREKQ FKNPKYPWTK APVFTGKIPM NMVSEKNSQA
260 270 280 290 300
IAALIIGDKN YNDNFITLRV WETMASDAVM LIDEEFDTKH RIINDARFYV
310 320 330 340 350
NNRAELIDRV NELKHSDVLR KEMLSIQHDI LNKTRAKKAE WQDAFKKAID

L
Length:351
Mass (Da):40,666
Last modified:August 13, 1987 - v1
Checksum:iD1F42B5FE6CB9D61
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 884KFMA → NLWQ in AAA88469. (PubMed:2832395)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03139 Genomic DNA. Translation: CAA26908.1.
AF158101 Genomic DNA. Translation: AAD42545.1.
M22767 Genomic DNA. Translation: AAA88469.1.
M69268 Genomic DNA. Translation: AAA32544.1.
Y00148 Genomic DNA. Translation: CAA68343.1.
PIRiA00576. XUBPB4.
RefSeqiNP_049658.1. NC_000866.4.

Genome annotation databases

GeneIDi1258765.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03139 Genomic DNA. Translation: CAA26908.1 .
AF158101 Genomic DNA. Translation: AAD42545.1 .
M22767 Genomic DNA. Translation: AAA88469.1 .
M69268 Genomic DNA. Translation: AAA32544.1 .
Y00148 Genomic DNA. Translation: CAA68343.1 .
PIRi A00576. XUBPB4.
RefSeqi NP_049658.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BGT X-ray 2.20 A 1-351 [» ]
1BGU X-ray 2.20 A 1-351 [» ]
1C3J X-ray 1.88 A 1-351 [» ]
1IXY X-ray 2.50 A/B 1-351 [» ]
1J39 X-ray 1.87 A 1-351 [» ]
1JEJ X-ray 2.50 A 1-351 [» ]
1JG6 X-ray 1.90 A 1-351 [» ]
1JG7 X-ray 1.65 A 1-351 [» ]
1JIU X-ray 2.50 A 1-351 [» ]
1JIV X-ray 2.07 A 1-351 [» ]
1JIX X-ray 1.65 A 1-351 [» ]
1M5R X-ray 1.80 A/B 1-351 [» ]
1NVK X-ray 1.80 A 1-351 [» ]
1NZD X-ray 2.00 A 1-351 [» ]
1NZF X-ray 2.10 A 1-351 [» ]
1QKJ X-ray 2.30 A 1-351 [» ]
1SXP X-ray 2.50 A/B 1-351 [» ]
1SXQ X-ray 1.80 A/B 1-351 [» ]
2BGT X-ray 2.20 A 1-351 [» ]
2BGU X-ray 2.20 A 1-351 [» ]
ProteinModelPortali P04547.
SMRi P04547. Positions 1-351.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GT63. Glycosyltransferase Family 63.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1258765.

Enzyme and pathway databases

UniPathwayi UPA00198 .

Miscellaneous databases

EvolutionaryTracei P04547.

Family and domain databases

InterProi IPR015281. Phage_T4_Bgt.
[Graphical view ]
Pfami PF09198. T4-Gluco-transf. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "T4-induced alpha- and beta-glucosyltransferase: cloning of the genes and a comparison of their products based on sequencing data."
    Tomaschewski J., Gram H., Crabb J.W., Rueger W.
    Nucleic Acids Res. 13:7551-7568(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Expression and DNA sequence of the cloned bacteriophage T4 dCMP hydroxymethylase gene."
    Thylen C.
    J. Bacteriol. 170:1994-1998(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
  4. "Nucleotide sequence of the deoxycytidylate hydroxymethylase gene of bacteriophage T4 (g42) and the homology of its gene product with thymidylate synthase of E. coli."
    Lamm N., Tomaschewski J., Rueger W.
    Nucleic Acids Res. 15:3920-3920(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
  5. "Identification of a family of bacteriophage T4 genes encoding proteins similar to those present in group I introns of fungi and phage."
    Sharma M., Ellis R.L., Hinton D.M.
    Proc. Natl. Acad. Sci. U.S.A. 89:6658-6662(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-351.
  6. "Biochemical characterization of recombinant beta-glucosyltransferase and analysis of global 5-hydroxymethylcytosine in unique genomes."
    Terragni J., Bitinaite J., Zheng Y., Pradhan S.
    Biochemistry 51:1009-1019(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Crystal structure of the DNA modifying enzyme beta-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose."
    Vrelink A., Rueger W., Driessen H.P.C., Freemont P.S.
    EMBO J. 13:3413-3422(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  8. "T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism."
    Morera S., Imberty A., Aschke-Sonnenborn U., Ruger W., Freemont P.S.
    J. Mol. Biol. 292:717-730(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiGSTB_BPT4
AccessioniPrimary (citable) accession number: P04547
Secondary accession number(s): Q38417
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3