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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

    • lipid glycosylation Source: InterPro
    • vancomycin biosynthetic process Source: UniProtKB
    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi13 – 131D → A: Decreased kcat, while it does not affect the KM for UDP-glucose. 1 Publication
    Mutagenesisi125 – 1251H → A: No decrease in catalytic rate. 1 Publication
    Mutagenesisi332 – 3321D → A: Strongly decreased activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 407407Vancomycin aglycone glucosyltransferasePRO_0000430437Add
    BLAST

    Structurei

    Secondary structure

    1
    407
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65Combined sources
    Helixi11 – 2616Combined sources
    Beta strandi30 – 356Combined sources
    Helixi37 – 393Combined sources
    Helixi40 – 456Combined sources
    Beta strandi50 – 523Combined sources
    Helixi69 – 9022Combined sources
    Turni91 – 933Combined sources
    Beta strandi95 – 1017Combined sources
    Helixi103 – 11614Combined sources
    Beta strandi120 – 1267Combined sources
    Helixi127 – 1293Combined sources
    Beta strandi133 – 1353Combined sources
    Helixi150 – 17627Combined sources
    Helixi185 – 1906Combined sources
    Turni200 – 2023Combined sources
    Helixi228 – 2358Combined sources
    Beta strandi241 – 2444Combined sources
    Helixi252 – 26413Combined sources
    Beta strandi269 – 2713Combined sources
    Helixi284 – 2863Combined sources
    Beta strandi287 – 2893Combined sources
    Helixi295 – 2984Combined sources
    Helixi299 – 3013Combined sources
    Beta strandi302 – 3076Combined sources
    Helixi311 – 32010Combined sources
    Beta strandi324 – 3263Combined sources
    Helixi333 – 34210Combined sources
    Beta strandi345 – 3484Combined sources
    Beta strandi350 – 3534Combined sources
    Helixi356 – 36611Combined sources
    Helixi369 – 38113Combined sources
    Helixi386 – 39914Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IIRX-ray1.80A1-407[»]
    ProteinModelPortaliP96559.
    SMRiP96559. Positions 1-401.
    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IIRX-ray1.80A1-407[»]
    ProteinModelPortaliP96559.
    SMRiP96559. Positions 1-401.
    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 11, 2015
    This is version 68 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.