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Protein

Vancomycin aglycone glucosyltransferase

Gene

gtfB

Organism
Amycolatopsis orientalis (Nocardia orientalis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Glucosyltransferase that transfers glucose to the 4-OH-Phegly4 residue of vancomycin aglycone (AGV) to produce devancoaminyl-vancomycin (DVV) in the biosynthesis of glycopeptide antibiotic chloroeremomycin, a member of the vancomycin group of antibiotics.2 Publications

Catalytic activityi

UDP-alpha-D-glucose + vancomycin aglycone = UDP + devancoaminyl-vancomycin.1 Publication

Kineticsi

kcat is 33 min(-1).

  1. KM=1.3 mM for UDP-glucose1 Publication

    Pathwayi: vancomycin biosynthesis

    This protein is involved in the pathway vancomycin biosynthesis, which is part of Antibiotic biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway vancomycin biosynthesis and in Antibiotic biosynthesis.

    GO - Molecular functioni

    • transferase activity, transferring hexosyl groups Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Enzyme and pathway databases

    BRENDAi2.4.1.310. 315.
    UniPathwayiUPA00162.

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vancomycin aglycone glucosyltransferase (EC:2.4.1.310)
    Alternative name(s):
    Glycosyltransferase GtfB
    Gene namesi
    Name:gtfB
    OrganismiAmycolatopsis orientalis (Nocardia orientalis)
    Taxonomic identifieri31958 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeAmycolatopsis

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi13D → A: Decreased kcat, while it does not affect the KM for UDP-glucose. 1 Publication1
    Mutagenesisi125H → A: No decrease in catalytic rate. 1 Publication1
    Mutagenesisi332D → A: Strongly decreased activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004304371 – 407Vancomycin aglycone glucosyltransferaseAdd BLAST407

    Structurei

    Secondary structure

    1407
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 6Combined sources5
    Helixi11 – 26Combined sources16
    Beta strandi30 – 35Combined sources6
    Helixi37 – 39Combined sources3
    Helixi40 – 45Combined sources6
    Beta strandi50 – 52Combined sources3
    Helixi69 – 90Combined sources22
    Turni91 – 93Combined sources3
    Beta strandi95 – 101Combined sources7
    Helixi103 – 116Combined sources14
    Beta strandi120 – 126Combined sources7
    Helixi127 – 129Combined sources3
    Beta strandi133 – 135Combined sources3
    Helixi150 – 176Combined sources27
    Helixi185 – 190Combined sources6
    Turni200 – 202Combined sources3
    Helixi228 – 235Combined sources8
    Beta strandi241 – 244Combined sources4
    Helixi252 – 264Combined sources13
    Beta strandi269 – 271Combined sources3
    Helixi284 – 286Combined sources3
    Beta strandi287 – 289Combined sources3
    Helixi295 – 298Combined sources4
    Helixi299 – 301Combined sources3
    Beta strandi302 – 307Combined sources6
    Helixi311 – 320Combined sources10
    Beta strandi324 – 326Combined sources3
    Helixi333 – 342Combined sources10
    Beta strandi345 – 348Combined sources4
    Beta strandi350 – 353Combined sources4
    Helixi356 – 366Combined sources11
    Helixi369 – 381Combined sources13
    Helixi386 – 399Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1IIRX-ray1.80A1-407[»]
    ProteinModelPortaliP96559.
    SMRiP96559.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP96559.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 28 family.Curated

    Phylogenomic databases

    KOiK16444.

    Family and domain databases

    InterProiIPR004276. GlycoTrans_28_N.
    IPR002213. UDP_glucos_trans.
    [Graphical view]
    PANTHERiPTHR11926. PTHR11926. 1 hit.
    PfamiPF03033. Glyco_transf_28. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P96559-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRVLLATCGS RGDTEPLVAL AVRVRDLGAD VRMCAPPDCA ERLAEVGVPH
    60 70 80 90 100
    VPVGPSARAP IQRAKPLTAE DVRRFTTEAI ATQFDEIPAA AEGCAAVVTT
    110 120 130 140 150
    GLLAAAIGVR SVAEKLGIPY FYAFHCPSYV PSPYYPPPPL GEPSTQDTID
    160 170 180 190 200
    IPAQWERNNQ SAYQRYGGLL NSHRDAIGLP PVEDIFTFGY TDHPWVAADP
    210 220 230 240 250
    VLAPLQPTDL DAVQTGAWIL PDERPLSPEL AAFLDAGPPP VYLGFGSLGA
    260 270 280 290 300
    PADAVRVAID AIRAHGRRVI LSRGWADLVL PDDGADCFAI GEVNHQVLFG
    310 320 330 340 350
    RVAAVIHHGG AGTTHVAARA GAPQILLPQM ADQPYYAGRV AELGVGVAHD
    360 370 380 390 400
    GPIPTFDSLS AALATALTPE THARATAVAG TIRTDGAAVA ARLLLDAVSR

    EKPTVSA
    Length:407
    Mass (Da):42,666
    Last modified:May 1, 1997 - v1
    Checksum:iDDCC0CF29A311201
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U84349 Genomic DNA. Translation: AAB49293.1.
    AJ223998 Genomic DNA. Translation: CAA11775.1.
    PIRiT30585.

    Genome annotation databases

    KEGGiag:CAA11775.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U84349 Genomic DNA. Translation: AAB49293.1.
    AJ223998 Genomic DNA. Translation: CAA11775.1.
    PIRiT30585.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1IIRX-ray1.80A1-407[»]
    ProteinModelPortaliP96559.
    SMRiP96559.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:CAA11775.

    Phylogenomic databases

    KOiK16444.

    Enzyme and pathway databases

    UniPathwayiUPA00162.
    BRENDAi2.4.1.310. 315.

    Miscellaneous databases

    EvolutionaryTraceiP96559.

    Family and domain databases

    InterProiIPR004276. GlycoTrans_28_N.
    IPR002213. UDP_glucos_trans.
    [Graphical view]
    PANTHERiPTHR11926. PTHR11926. 1 hit.
    PfamiPF03033. Glyco_transf_28. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGTFB_AMYOR
    AccessioniPrimary (citable) accession number: P96559
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 2014
    Last sequence update: May 1, 1997
    Last modified: November 30, 2016
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In A.orientalis different glycosyltransferases are involved in biosynthesis of the vancomycin group of antibiotics. GtfA (AC P96558), GtfB and GtfC (AC P96560) are involved in biosynthesis of antibiotic chloroeremomycin, while GtfD (AC Q9AFC7) and GtfE (AC G4V4R9) are involved in biosynthesis of vancomycin.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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.