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Protein

Demethylrebeccamycin-D-glucose O-methyltransferase

Gene

rebM

Organism
Lechevalieria aerocolonigenes (Nocardia aerocolonigenes) (Saccharothrix aerocolonigenes)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Glycosyl O-methyltransferase that catalyzes the final step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid that inhibits topoisomerase 1. Has broad substrate specificity and functions as glycosyl O-methyltransferase on a number of rebeccamycin analogs.2 Publications

Catalytic activityi

4'-demethylrebeccamycin + S-adenosyl-L-methionine = rebeccamycin + S-adenosyl-L-homocysteine.1 Publication

Kineticsi

  1. KM=12 µM for S-adenosyl-L-methionine2 Publications

    pH dependencei

    Optimum pH is 6.5-8.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei101 – 1011S-adenosyl-L-methionineCombined sources1 Publication
    Binding sitei106 – 1061S-adenosyl-L-methionineCombined sources1 Publication
    Binding sitei146 – 1461S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication
    Sitei150 – 1501Important for catalysis
    Binding sitei151 – 1511S-adenosyl-L-methionine1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDAi2.1.1.164. 4340.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Demethylrebeccamycin-D-glucose O-methyltransferase (EC:2.1.1.1641 Publication)
    Alternative name(s):
    Rebeccamycin O-methyltransferase
    Rebeccamycin sugar 4'-O-methyltransferase RebM
    Gene namesi
    Name:rebM
    OrganismiLechevalieria aerocolonigenes (Nocardia aerocolonigenes) (Saccharothrix aerocolonigenes)
    Taxonomic identifieri68170 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeLechevalieria

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851P → S: Reduces enzyme activity by 87%. Strongly reduced affinity for S-adenosyl-L-methionine. 1 Publication
    Mutagenesisi146 – 1461L → V: Reduces enzyme activity by 45%. Reduces affinity for S-adenosyl-L-methionine. 1 Publication
    Mutagenesisi148 – 1481S → A: Reduces enzyme activity by 50%. 1 Publication
    Mutagenesisi150 – 1501H → A: Reduces enzyme activity by 95%. Slightly reduced affinity for S-adenosyl-L-methionine. Loss of enzyme activity; when associated with A-151. 1 Publication
    Mutagenesisi151 – 1511H → A: Reduces enzyme activity by 80%. Strongly reduced affinity for S-adenosyl-L-methionine. Loss of enzyme activity; when associated with A-150. 1 Publication
    Mutagenesisi176 – 1761D → A: Reduces enzyme activity by 90%. Strongly reduced affinity for S-adenosyl-L-methionine. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 283283Demethylrebeccamycin-D-glucose O-methyltransferasePRO_0000415892Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 373Combined sources
    Helixi52 – 6615Combined sources
    Beta strandi74 – 796Combined sources
    Helixi84 – 929Combined sources
    Beta strandi96 – 1027Combined sources
    Helixi104 – 11613Combined sources
    Turni120 – 1223Combined sources
    Beta strandi123 – 1275Combined sources
    Beta strandi140 – 1478Combined sources
    Turni149 – 1513Combined sources
    Helixi155 – 1639Combined sources
    Beta strandi166 – 18116Combined sources
    Helixi185 – 19814Combined sources
    Helixi206 – 21510Combined sources
    Beta strandi219 – 2257Combined sources
    Helixi227 – 2304Combined sources
    Helixi233 – 24311Combined sources
    Helixi245 – 2528Combined sources
    Helixi254 – 26815Combined sources
    Beta strandi273 – 2819Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BUSX-ray2.65A/B12-283[»]
    ProteinModelPortaliQ8KZ94.
    SMRiQ8KZ94. Positions 33-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8KZ94.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 1302S-adenosyl-L-methionine bindingCombined sources1 Publication

    Sequence similaritiesi

    Belongs to the methyltransferase superfamily.Curated

    Phylogenomic databases

    KOiK19889.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR013216. Methyltransf_11.
    IPR020803. PKS_MeTfrase.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PfamiPF08241. Methyltransf_11. 1 hit.
    [Graphical view]
    SMARTiSM00828. PKS_MT. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8KZ94-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTESKSEGTA VAAPTPEEVR QMYDDFTDPF ARIWGENLHF GYWEDAGADV
    60 70 80 90 100
    SVDDATDRLT DEMIALLDVR SGDRVLDVGC GIGKPAVRLA TARDVRVTGI
    110 120 130 140 150
    SISRPQVNQA NARATAAGLA NRVTFSYADA MDLPFEDASF DAVWALESLH
    160 170 180 190 200
    HMPDRGRALR EMARVLRPGG TVAIADFVLL APVEGAKKEA VDAFRAGGGV
    210 220 230 240 250
    LSLGGIDEYE SDVRQAELVV TSTVDISAQA RPSLVKTAEA FENARSQVEP
    260 270 280
    FMGAEGLDRM IATFRGLAEV PEAGYVLIGA RKP
    Length:283
    Mass (Da):30,374
    Last modified:October 1, 2002 - v1
    Checksum:i3A442B1545477CC6
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB090952 Genomic DNA. Translation: BAC10678.1.

    Genome annotation databases

    KEGGiag:BAC10678.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB090952 Genomic DNA. Translation: BAC10678.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BUSX-ray2.65A/B12-283[»]
    ProteinModelPortaliQ8KZ94.
    SMRiQ8KZ94. Positions 33-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAC10678.

    Phylogenomic databases

    KOiK19889.

    Enzyme and pathway databases

    BRENDAi2.1.1.164. 4340.

    Miscellaneous databases

    EvolutionaryTraceiQ8KZ94.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR013216. Methyltransf_11.
    IPR020803. PKS_MeTfrase.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PfamiPF08241. Methyltransf_11. 1 hit.
    [Graphical view]
    SMARTiSM00828. PKS_MT. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiREBMT_NOCAE
    AccessioniPrimary (citable) accession number: Q8KZ94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2012
    Last sequence update: October 1, 2002
    Last modified: September 7, 2016
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.