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Protein

dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase

Gene

tylM1

Organism
Streptomyces fradiae (Streptomyces roseoflavus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of mycaminose, an essential structural component of the macrolide antibiotic tylosin. Involved in the last step in mycaminose biosynthesis by mediating dimethylation of the hexose C-3' amino group.3 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose = 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose.1 Publication

Kineticsi

kcat is 7.2 min(-1) with dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose as substrate. kcat is 32.5 min(-1) with TDP-3-N-methylamino-3,6-dideoxy-R-D-glucopyranose as substrate. kcat is 9.9 min(-1) with dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose as substrate.

  1. KM=118.4 µM for dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose1 Publication
  2. KM=46.8 µM for TDP-3-N-methylamino-3,6-dideoxy-R-D-glucopyranose1 Publication
  3. KM=59.4 µM for dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose1 Publication

    Pathwayi: tylosin biosynthesis

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei14 – 141S-adenosyl-L-methionine1 Publication
    Binding sitei22 – 221S-adenosyl-L-methionine1 Publication
    Binding sitei33 – 331S-adenosyl-L-methionine1 Publication
    Binding sitei58 – 581S-adenosyl-L-methionine; via carbonyl oxygen1 Publication
    Binding sitei79 – 791S-adenosyl-L-methionine1 Publication
    Binding sitei117 – 1171S-adenosyl-L-methionine; via carbonyl oxygen1 Publication

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB
    • S-adenosylmethionine-dependent methyltransferase activity Source: UniProtKB

    GO - Biological processi

    • antibiotic biosynthetic process Source: UniProtKB
    • methylation Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18381.
    BRENDAi2.1.1.235. 5932.
    UniPathwayiUPA01018.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase (EC:2.1.1.235)
    Alternative name(s):
    Tylosin biosynthesis protein M1
    Gene namesi
    Name:tylM1
    Synonyms:tylMI
    OrganismiStreptomyces fradiae (Streptomyces roseoflavus)
    Taxonomic identifieri1906 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi123 – 1231H → A or N: Strongly reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 255254dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferasePRO_0000418453Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Structurei

    Secondary structure

    1
    255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 2813Combined sources
    Helixi33 – 4715Combined sources
    Beta strandi53 – 575Combined sources
    Helixi63 – 686Combined sources
    Turni69 – 713Combined sources
    Beta strandi72 – 809Combined sources
    Helixi82 – 9110Combined sources
    Beta strandi95 – 995Combined sources
    Turni102 – 1043Combined sources
    Beta strandi111 – 1166Combined sources
    Helixi120 – 1234Combined sources
    Helixi126 – 13914Combined sources
    Beta strandi141 – 1499Combined sources
    Turni155 – 1573Combined sources
    Beta strandi162 – 1709Combined sources
    Beta strandi173 – 18412Combined sources
    Beta strandi187 – 19812Combined sources
    Turni199 – 2013Combined sources
    Beta strandi202 – 21312Combined sources
    Helixi217 – 22610Combined sources
    Beta strandi229 – 2368Combined sources
    Turni237 – 2393Combined sources
    Beta strandi243 – 2486Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PFGX-ray1.35A1-255[»]
    3PFHX-ray1.79A/D1-255[»]
    3PX2X-ray1.65A/D1-255[»]
    3PX3X-ray1.80A/D1-255[»]
    4OQDX-ray1.60A/B/C/D1-255[»]
    4OQEX-ray2.20A/B1-255[»]
    ProteinModelPortaliP95748.
    SMRiP95748. Positions 14-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP95748.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 592S-adenosyl-L-methionine binding
    Regioni101 – 1022S-adenosyl-L-methionine binding

    Domaini

    His-123 is a strong candicate for an active site that hydrogen bonds to a water molecule which in turn hydrogen bonds to the C-3' amino group. However, it is not conserved in related S.venezuelae DesVI methyltransferase and its mutagenesis does not completely abolish catalytic activity (PubMed:21142177).1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    KOiK13307.

    Family and domain databases

    Gene3Di3.40.50.150. 2 hits.
    InterProiIPR029063. SAM-dependent_MTases.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P95748-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAHSSATAGP QADYSGEIAE LYDLVHQGKG KDYHREAADL AALVRRHSPK
    60 70 80 90 100
    AASLLDVACG TGMHLRHLAD SFGTVEGLEL SADMLAIARR RNPDAVLHHG
    110 120 130 140 150
    DMRDFSLGRR FSAVTCMFSS IGHLAGQAEL DAALERFAAH VLPDGVVVVE
    160 170 180 190 200
    PWWFPENFTP GYVAAGTVEA GGTTVTRVSH SSREGEATRI EVHYLVAGPD
    210 220 230 240 250
    RGITHHEESH RITLFTREQY ERAFTAAGLS VEFMPGGPSG RGLFTGLPGA

    KGETR
    Length:255
    Mass (Da):27,428
    Last modified:November 1, 1999 - v2
    Checksum:i74C1034DA07FA07A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X81885 Genomic DNA. Translation: CAA57473.2.
    RefSeqiWP_050364681.1. NZ_LGSP01000138.1.

    Genome annotation databases

    KEGGiag:CAA57473.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X81885 Genomic DNA. Translation: CAA57473.2.
    RefSeqiWP_050364681.1. NZ_LGSP01000138.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PFGX-ray1.35A1-255[»]
    3PFHX-ray1.79A/D1-255[»]
    3PX2X-ray1.65A/D1-255[»]
    3PX3X-ray1.80A/D1-255[»]
    4OQDX-ray1.60A/B/C/D1-255[»]
    4OQEX-ray2.20A/B1-255[»]
    ProteinModelPortaliP95748.
    SMRiP95748. Positions 14-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:CAA57473.

    Phylogenomic databases

    KOiK13307.

    Enzyme and pathway databases

    UniPathwayiUPA01018.
    BioCyciMetaCyc:MONOMER-18381.
    BRENDAi2.1.1.235. 5932.

    Miscellaneous databases

    EvolutionaryTraceiP95748.

    Family and domain databases

    Gene3Di3.40.50.150. 2 hits.
    InterProiIPR029063. SAM-dependent_MTases.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiTYLM1_STRFR
    AccessioniPrimary (citable) accession number: P95748
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: November 1, 1999
    Last modified: March 16, 2016
    This is version 62 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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.