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Protein
Submitted name:

Putative glycosyltransferase

Gene

vldE

Organism
Streptomyces hygroscopicus subsp. limoneus
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi114 – 1141Magnesium 4Combined sources
Metal bindingi187 – 1871Magnesium 3Combined sources
Metal bindingi218 – 2181Magnesium 4Combined sources
Metal bindingi287 – 2871Magnesium 3; via pros nitrogenCombined sources
Metal bindingi321 – 3211Magnesium 3; via carbonyl oxygenCombined sources
Metal bindingi412 – 4121Magnesium 4Combined sources

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. trehalose biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

TransferaseImported

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13774.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
Submitted name:
Putative glycosyltransferaseImported
Gene namesi
Name:vldEImported
OrganismiStreptomyces hygroscopicus subsp. limoneusImported
Taxonomic identifieri264445 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T5TX-ray1.70A/B2-497[»]
3T7DX-ray1.70A/B2-497[»]
3VDMX-ray1.98A/B1-497[»]
3VDNX-ray2.55B1-497[»]
4F96X-ray2.15A/B1-497[»]
4F97X-ray2.11A/B1-497[»]
4F9FX-ray2.81A/B/C/D/E/F1-497[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

InterProiIPR001830. Glyco_trans_20.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15JG1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTGSEIFLAS KRAAITYDTD PATGEPRAWL APGGTGNVVA EQAGVLNISW
60 70 80 90 100
IASADSEDDR RASALNPDGV TMELHSGREI LVRLIRHDPA VFRNVQNFMT
110 120 130 140 150
ANLMWAANNY GWDRWTQPSF GSDAREGWAD FGRFTRDFAD AILKSSAQSA
160 170 180 190 200
DPVYLVHDYQ LVGVPALLRE QRPDAPILLF VHIPWPSADY WRILPKEIRT
210 220 230 240 250
GILHGMLPAT TIGFFADRWC RNFLESVADL LPDARIDREA MTVEWRGHRT
260 270 280 290 300
RLRTMPLGYS PLTLDGRNPQ LPEGIEEWAD GHRLVVHSGR TDPIKNAERA
310 320 330 340 350
VRAFVLAARG GGLEKTRMLV RMNPNRLYVP ANADYVHRVE TAVAEANAEL
360 370 380 390 400
GSDTVRIDND NDVNHTIACF RRADLLIFNS TVDGQNLSTF EAPLVNERDA
410 420 430 440 450
DVILSETCGA AEVLGEYCRS VNPFDLVEQA EAISAALAAG PRQRAEAAAR
460 470 480 490
RRDAARPWTL EAWVQAQLDG LAADHAARTA TAERFDTAPA VSTRADL
Length:497
Mass (Da):54,943
Last modified:July 25, 2006 - v1
Checksum:i91CDAB5D51B859DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ223652 Genomic DNA. Translation: ABC67269.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ223652 Genomic DNA. Translation: ABC67269.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T5TX-ray1.70A/B2-497[»]
3T7DX-ray1.70A/B2-497[»]
3VDMX-ray1.98A/B1-497[»]
3VDNX-ray2.55B1-497[»]
4F96X-ray2.15A/B1-497[»]
4F97X-ray2.11A/B1-497[»]
4F9FX-ray2.81A/B/C/D/E/F1-497[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13774.

Family and domain databases

InterProiIPR001830. Glyco_trans_20.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genetic localization and heterologous expression of validamycin biosynthetic gene cluster isolated from Streptomyces hygroscopicus var. limoneus KCCM 11405 (IFO 12704)."
    Singh D., Seo M.J., Kwon H.J., Rajkarnikar A., Kim K.R., Kim S.O., Suh J.W.
    Gene 376:13-23(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: KCCM 11405Imported.
  2. "Structural basis for the substrate specificity of ValL."
    Zhang H., Zheng L., Qian H.
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-497 IN COMPLEX WITH MAGNESIUM.
  3. "Structural basis for the substrate specificity of ValL."
    Zhang H., Zheng L., Qian H., Chen J.
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-497 IN COMPLEX WITH MAGNESIUM.
  4. "Mechanistic insights into validoxylamine A 7'-phosphate synthesis by VldE using the structure of the entire product complex."
    Cavalier M.C., Yim Y.S., Asamizu S., Neau D., Almabruk K.H., Mahmud T., Lee Y.H.
    PLoS ONE 7:e44934-e44934(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS).
  5. "Crystal Structure of the VldE, the pseudo-glycosyltransferase, which catalyzes non-glycosidic C-N coupling in Validamycin A biosynthesis."
    Cavalier M.C., Yim Y.-S., Asamizu S., Neau D., Mahmud T., Lee Y.-H.
    Submitted (JAN-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
  6. "Crystal Structure of VldE, the pseudo-glycosyltransferase which catalyzes non-glycosidic C-N coupling in Validamycin A biosynthesis."
    Cavalier M.C., Yim Y.-S., Asamizu S., Neau D., Mahmud T., Lee Y.-H.
    Submitted (JAN-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).

Entry informationi

Entry nameiQ15JG1_STRHY
AccessioniPrimary (citable) accession number: Q15JG1
Entry historyi
Integrated into UniProtKB/TrEMBL: July 25, 2006
Last sequence update: July 25, 2006
Last modified: January 7, 2015
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.