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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)DescriptionActionsGraphical viewLength
    Binding sitei101S-adenosyl-L-methionineCombined sources1 Publication1
    Binding sitei106S-adenosyl-L-methionineCombined sources1 Publication1
    Binding sitei146S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
    Sitei150Important for catalysis1
    Binding sitei151S-adenosyl-L-methionine1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi85P → S: Reduces enzyme activity by 87%. Strongly reduced affinity for S-adenosyl-L-methionine. 1 Publication1
    Mutagenesisi146L → V: Reduces enzyme activity by 45%. Reduces affinity for S-adenosyl-L-methionine. 1 Publication1
    Mutagenesisi148S → A: Reduces enzyme activity by 50%. 1 Publication1
    Mutagenesisi150H → A: Reduces enzyme activity by 95%. Slightly reduced affinity for S-adenosyl-L-methionine. Loss of enzyme activity; when associated with A-151. 1 Publication1
    Mutagenesisi151H → A: Reduces enzyme activity by 80%. Strongly reduced affinity for S-adenosyl-L-methionine. Loss of enzyme activity; when associated with A-150. 1 Publication1
    Mutagenesisi176D → A: Reduces enzyme activity by 90%. Strongly reduced affinity for S-adenosyl-L-methionine. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004158921 – 283Demethylrebeccamycin-D-glucose O-methyltransferaseAdd BLAST283

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1283
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi35 – 37Combined sources3
    Helixi52 – 66Combined sources15
    Beta strandi74 – 79Combined sources6
    Helixi84 – 92Combined sources9
    Beta strandi96 – 102Combined sources7
    Helixi104 – 116Combined sources13
    Turni120 – 122Combined sources3
    Beta strandi123 – 127Combined sources5
    Beta strandi140 – 147Combined sources8
    Turni149 – 151Combined sources3
    Helixi155 – 163Combined sources9
    Beta strandi166 – 181Combined sources16
    Helixi185 – 198Combined sources14
    Helixi206 – 215Combined sources10
    Beta strandi219 – 225Combined sources7
    Helixi227 – 230Combined sources4
    Helixi233 – 243Combined sources11
    Helixi245 – 252Combined sources8
    Helixi254 – 268Combined sources15
    Beta strandi273 – 281Combined sources9

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ8KZ94.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni129 – 130S-adenosyl-L-methionine bindingCombined sources1 Publication2

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3BUSX-ray2.65A/B12-283[»]
    ProteinModelPortaliQ8KZ94.
    SMRiQ8KZ94.
    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: November 30, 2016
    This is version 54 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.