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Protein

DNA alpha-glucosyltransferase

Gene

agt

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

Functioni

Catalyzes the transfer of glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine of T4 DNA to yield glucosyl 5-hydroxymethyl cytosine (glc-HMC) (PubMed:15381072). This DNA process seems to occur immediately after DNA synthesis since the DNA alpha-glucosyltransferase interacts with the clamp protein gp45 (PubMed:15381072). The glc-HMC modification protects the phage genome against its own nucleases and the host restriction endonuclease system (PubMed:15381072). The glc-HMC modification also protects against the host CRISPR-Cas9 defense system (PubMed:26081634).2 Publications

Catalytic activityi

Transfers an alpha-D-glucosyl residue from UDP-glucose to a hydroxymethylcytosine residue in DNA.1 Publication

Pathwayi: DNA modification

This protein is involved in the pathway DNA modification, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA modification and in Genetic information processing.

GO - Molecular functioni

  • DNA alpha-glucosyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

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

Enzyme and pathway databases

UniPathwayiUPA00198.

Protein family/group databases

CAZyiGT72. Glycosyltransferase Family 72.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA alpha-glucosyltransferase (EC:2.4.1.261 Publication)
Short name:
AGT
Short name:
Alpha-GT
Gene namesi
Name:agt
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000009087 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400DNA alpha-glucosyltransferasePRO_0000164941Add
BLAST

Interactioni

Subunit structurei

Interacts with clamp protein gp45.2 Publications

Structurei

Secondary structure

1
400
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi15 – 2915Combined sources
Beta strandi33 – 397Combined sources
Turni45 – 484Combined sources
Beta strandi49 – 513Combined sources
Turni53 – 553Combined sources
Beta strandi57 – 593Combined sources
Turni61 – 633Combined sources
Helixi65 – 728Combined sources
Beta strandi76 – 827Combined sources
Helixi90 – 10213Combined sources
Beta strandi107 – 1137Combined sources
Helixi118 – 1214Combined sources
Beta strandi124 – 1263Combined sources
Helixi127 – 1337Combined sources
Beta strandi135 – 1406Combined sources
Beta strandi142 – 1443Combined sources
Helixi145 – 1484Combined sources
Helixi150 – 1545Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi171 – 1733Combined sources
Helixi180 – 1878Combined sources
Helixi191 – 1933Combined sources
Beta strandi195 – 2028Combined sources
Helixi207 – 2093Combined sources
Helixi211 – 22010Combined sources
Turni221 – 2266Combined sources
Beta strandi228 – 2325Combined sources
Helixi238 – 2458Combined sources
Beta strandi250 – 2534Combined sources
Helixi255 – 2606Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi269 – 2735Combined sources
Helixi277 – 2859Combined sources
Beta strandi287 – 2926Combined sources
Helixi298 – 3003Combined sources
Helixi307 – 3159Combined sources
Beta strandi317 – 3226Combined sources
Helixi323 – 3286Combined sources
Turni332 – 3343Combined sources
Helixi338 – 3403Combined sources
Beta strandi346 – 3483Combined sources
Helixi350 – 3523Combined sources
Helixi353 – 36412Combined sources
Helixi367 – 38519Combined sources
Helixi387 – 39812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XV5X-ray1.73A1-400[»]
1Y6FX-ray2.40A/B1-400[»]
1Y6GX-ray2.80A/B1-400[»]
1Y8ZX-ray1.90A/B1-400[»]
1YA6X-ray2.40A/B1-400[»]
ProteinModelPortaliP04519.
SMRiP04519. Positions 1-400.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04519.

Family & Domainsi

Family and domain databases

InterProiIPR016223. DNA_alpha-glucosyltransferase.
[Graphical view]
PfamiPF11440. AGT. 1 hit.
[Graphical view]
PIRSFiPIRSF000471. DNA_alpha-glucosyltransferase. 1 hit.

Sequencei

Sequence statusi: Complete.

P04519-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRICIFMARG LEGCGVTKFS LEQRDWFIKN GHEVTLVYAK DKSFTRTSSH
60 70 80 90 100
DHKSFSIPVI LAKEYDKALK LVNDCDILII NSVPATSVQE ATINNYKKLL
110 120 130 140 150
DNIKPSIRVV VYQHDHSVLS LRRNLGLEET VRRADVIFSH SDNGDFNKVL
160 170 180 190 200
MKEWYPETVS LFDDIEEAPT VYNFQPPMDI VKVRSTYWKD VSEINMNINR
210 220 230 240 250
WIGRTTTWKG FYQMFDFHEK FLKPAGKSTV MEGLERSPAF IAIKEKGIPY
260 270 280 290 300
EYYGNREIDK MNLAPNQPAQ ILDCYINSEM LERMSKSGFG YQLSKLNQKY
310 320 330 340 350
LQRSLEYTHL ELGACGTIPV FWKSTGENLK FRVDNTPLTS HDSGIIWFDE
360 370 380 390 400
NDMESTFERI KELSSDRALY DREREKAYEF LYQHQDSSFC FKEQFDIITK
Length:400
Mass (Da):46,704
Last modified:August 13, 1987 - v1
Checksum:i09CC1D4800F5AD2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01804 Genomic DNA. Translation: CAA25940.1.
M10160 Genomic DNA. Translation: AAC05390.1.
AF158101 Genomic DNA. Translation: AAD42527.1.
PIRiA00577. XUBPA4.
RefSeqiNP_049673.1. NC_000866.4.

Genome annotation databases

GeneIDi1258823.
KEGGivg:1258823.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01804 Genomic DNA. Translation: CAA25940.1.
M10160 Genomic DNA. Translation: AAC05390.1.
AF158101 Genomic DNA. Translation: AAD42527.1.
PIRiA00577. XUBPA4.
RefSeqiNP_049673.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XV5X-ray1.73A1-400[»]
1Y6FX-ray2.40A/B1-400[»]
1Y6GX-ray2.80A/B1-400[»]
1Y8ZX-ray1.90A/B1-400[»]
1YA6X-ray2.40A/B1-400[»]
ProteinModelPortaliP04519.
SMRiP04519. Positions 1-400.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT72. Glycosyltransferase Family 72.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258823.
KEGGivg:1258823.

Enzyme and pathway databases

UniPathwayiUPA00198.

Miscellaneous databases

EvolutionaryTraceiP04519.

Family and domain databases

InterProiIPR016223. DNA_alpha-glucosyltransferase.
[Graphical view]
PfamiPF11440. AGT. 1 hit.
[Graphical view]
PIRSFiPIRSF000471. DNA_alpha-glucosyltransferase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genes 55, alpha gt, 47 and 46 of bacteriophage T4: the genomic organization as deduced by sequence analysis."
    Gram H., Rueger W.
    EMBO J. 4:257-264(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "On the specificity of bacteriophage-induced hydroxymethylcytosine glucosyltransferases. II. Specificities of hydroxymethylcytosine alphaand beta-glucosyltransferases induced by bacteriophage T4."
    de Waard A., Ubbink T.E., Beukman W.
    Eur. J. Biochem. 2:303-308(1967) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  4. "Bacteriophage T4 alpha-glucosyltransferase: a novel interaction with gp45 and aspects of the catalytic mechanism."
    Sommer N., Depping R., Piotrowski M., Ruger W.
    Biochem. Biophys. Res. Commun. 323:809-815(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GP45.
  5. "Covalent Modification of Bacteriophage T4 DNA Inhibits CRISPR-Cas9."
    Bryson A.L., Hwang Y., Sherrill-Mix S., Wu G.D., Lewis J.D., Black L., Clark T.A., Bushman F.D.
    MBio 6:E00648-E00648(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase."
    Lariviere L., Sommer N., Morera S.
    J. Mol. Biol. 352:139-150(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.

Entry informationi

Entry nameiGSTA_BPT4
AccessioniPrimary (citable) accession number: P04519
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 8, 2016
This is version 84 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

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.