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Protein

Mitomycin biosynthesis 6-O-methyltransferase

Gene

mmcR

Organism
Streptomyces lavendulae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the quinone methoxy group present in the mitomycin A and B, which are used as anticancer agents (PubMed:10099135, PubMed:17461583). In vitro, catalyzes the 6-O-methylation of both C9-beta- and C9-alpha-configured 6-hydroxymitomycins via the transfer of the S-methyl group of S-adenosyl-L-methionine (AdoMet) to the 6-demethylmitomycin A and B. It can also use hydroxyquinone as substrate (PubMed:17461583).2 Publications

Catalytic activityi

S-adenosyl-L-methionine + 6-demethylmitomycin A = S-adenosyl-L- homocysteine + mitomycin A.1 Publication
S-adenosyl-L-methionine + 6-demethylmitomycin B = S-adenosyl-L- homocysteine + mitomycin B.1 Publication

Enzyme regulationi

Completely inhibited by Zn2+ and Cu2+.1 Publication

Kineticsi

Kcat is 0.110 min(-1) for methyltransferase activity with S-adenosyl-L-methionine as substrate. Kcat is 0.103 min(-1) for methyltransferase activity with 6-demethylmitomycin A as substrate.1 Publication

  1. KM=3.8 µM for S-adenosyl-L-methionine1 Publication
  2. KM=170 µM for 6-demethylmitomycin A1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei167 – 1671S-adenosyl-L-homocysteine1 Publication
    Binding sitei190 – 1901S-adenosyl-L-homocysteine; via carbonyl oxygen1 Publication
    Binding sitei255 – 2551S-adenosyl-L-homocysteine1 Publication
    Active sitei259 – 2591Proton acceptor1 Publication
    Binding sitei288 – 2881Substrate1 Publication

    GO - Molecular functioni

    • methyltransferase activity Source: UniProtKB
    • O-methyltransferase activity Source: CACAO

    GO - Biological processi

    • quinone biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitomycin biosynthesis 6-O-methyltransferaseCurated (EC:2.1.1.3161 Publication)
    Alternative name(s):
    Mitomycin 7-O-methyltransferase1 Publication
    Gene namesi
    Name:mmcR1 Publication
    OrganismiStreptomyces lavendulae
    Taxonomic identifieri1914 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene are unable to produce mitomycins A and B, and accumulate 6-demethylmitomycin A and 6-demethylmitomycin B.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 349349Mitomycin biosynthesis 6-O-methyltransferasePRO_0000435507Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    349
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 4130Combined sources
    Helixi44 – 474Combined sources
    Helixi54 – 618Combined sources
    Helixi65 – 7713Combined sources
    Beta strandi80 – 834Combined sources
    Beta strandi89 – 913Combined sources
    Helixi94 – 974Combined sources
    Helixi106 – 11510Combined sources
    Helixi117 – 1248Combined sources
    Helixi126 – 1327Combined sources
    Helixi137 – 1415Combined sources
    Helixi145 – 1517Combined sources
    Helixi153 – 17725Combined sources
    Beta strandi184 – 1896Combined sources
    Helixi195 – 2039Combined sources
    Beta strandi208 – 2136Combined sources
    Helixi215 – 22713Combined sources
    Turni231 – 2333Combined sources
    Beta strandi234 – 2385Combined sources
    Turni241 – 2433Combined sources
    Beta strandi250 – 2567Combined sources
    Helixi258 – 2603Combined sources
    Helixi263 – 27412Combined sources
    Beta strandi282 – 2898Combined sources
    Helixi296 – 30914Combined sources
    Helixi316 – 3249Combined sources
    Turni325 – 3273Combined sources
    Beta strandi328 – 3358Combined sources
    Beta strandi337 – 34812Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GWZX-ray1.91A/B/C/D2-349[»]
    3GXOX-ray2.30A/B/C/D2-349[»]
    ProteinModelPortaliQ9X5T6.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X5T6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni213 – 2142S-adenosyl-L-homocysteine binding1 Publication
    Regioni240 – 2412S-adenosyl-L-homocysteine binding1 Publication

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.40.50.150. 1 hit.
    InterProiIPR016461. O-MeTrfase_COMT.
    IPR001077. O_MeTrfase_2.
    IPR029063. SAM-dependent_MTases.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00891. Methyltransf_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005739. O-mtase. 1 hit.
    SUPFAMiSSF46785. SSF46785. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEiPS51683. SAM_OMT_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9X5T6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTVEQTPENP GTAARAAAEE TVNDILQGAW KARAIHVAVE LGVPELLQEG
    60 70 80 90 100
    PRTATALAEA TGAHEQTLRR LLRLLATVGV FDDLGHDDLF AQNALSAVLL
    110 120 130 140 150
    PDPASPVATD ARFQAAPWHW RAWEQLTHSV RTGEASFDVA NGTSFWQLTH
    160 170 180 190 200
    EDPKARELFN RAMGSVSLTE AGQVAAAYDF SGAATAVDIG GGRGSLMAAV
    210 220 230 240 250
    LDAFPGLRGT LLERPPVAEE ARELLTGRGL ADRCEILPGD FFETIPDGAD
    260 270 280 290 300
    VYLIKHVLHD WDDDDVVRIL RRIATAMKPD SRLLVIDNLI DERPAASTLF
    310 320 330 340
    VDLLLLVLVG GAERSESEFA ALLEKSGLRV ERSLPCGAGP VRIVEIRRA
    Length:349
    Mass (Da):37,628
    Last modified:December 12, 2006 - v2
    Checksum:i34F43D4279A60881
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF127374 Genomic DNA. Translation: AAD32742.2.

    Genome annotation databases

    KEGGiag:AAD32742.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF127374 Genomic DNA. Translation: AAD32742.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GWZX-ray1.91A/B/C/D2-349[»]
    3GXOX-ray2.30A/B/C/D2-349[»]
    ProteinModelPortaliQ9X5T6.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAD32742.

    Miscellaneous databases

    EvolutionaryTraceiQ9X5T6.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.40.50.150. 1 hit.
    InterProiIPR016461. O-MeTrfase_COMT.
    IPR001077. O_MeTrfase_2.
    IPR029063. SAM-dependent_MTases.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00891. Methyltransf_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005739. O-mtase. 1 hit.
    SUPFAMiSSF46785. SSF46785. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEiPS51683. SAM_OMT_II. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMMCR_STRLA
    AccessioniPrimary (citable) accession number: Q9X5T6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 17, 2016
    Last sequence update: December 12, 2006
    Last modified: July 6, 2016
    This is version 87 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

    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.