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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)DescriptionActionsGraphical viewLength
    Binding sitei14S-adenosyl-L-methionine1 Publication1
    Binding sitei22S-adenosyl-L-methionine1 Publication1
    Binding sitei33S-adenosyl-L-methionine1 Publication1
    Binding sitei58S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
    Binding sitei79S-adenosyl-L-methionine1 Publication1
    Binding sitei117S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi123H → A or N: Strongly reduced activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00004184532 – 255dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferaseAdd BLAST254

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Structurei

    Secondary structure

    1255
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi16 – 28Combined sources13
    Helixi33 – 47Combined sources15
    Beta strandi53 – 57Combined sources5
    Helixi63 – 68Combined sources6
    Turni69 – 71Combined sources3
    Beta strandi72 – 80Combined sources9
    Helixi82 – 91Combined sources10
    Beta strandi95 – 99Combined sources5
    Turni102 – 104Combined sources3
    Beta strandi111 – 116Combined sources6
    Helixi120 – 123Combined sources4
    Helixi126 – 139Combined sources14
    Beta strandi141 – 149Combined sources9
    Turni155 – 157Combined sources3
    Beta strandi162 – 170Combined sources9
    Beta strandi173 – 184Combined sources12
    Beta strandi187 – 198Combined sources12
    Turni199 – 201Combined sources3
    Beta strandi202 – 213Combined sources12
    Helixi217 – 226Combined sources10
    Beta strandi229 – 236Combined sources8
    Turni237 – 239Combined sources3
    Beta strandi243 – 248Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP95748.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni58 – 59S-adenosyl-L-methionine binding2
    Regioni101 – 102S-adenosyl-L-methionine binding2

    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
    PDB 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.
    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: November 2, 2016
    This is version 64 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.