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Protein

2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase

Gene

ncsB1

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

Functioni

S-adenosyl-L-methionine-dependent O-methyltransferase that catalyzes regiospecific methylation at the 7-hydroxy group of 2,7-dihydroxy-5-methyl-1-naphthoate in the biosynthesis of the naphthoate moiety of the neocarzinostatin chromophore. Also recognizes other dihydroxynaphthoate as substrates and catalyzes their regiospecific O-methylation. The carboxylate and its ortho-hydroxy groups of the substrate appear to be crucial for NcsB1 substrate recognition and binding, and O-methylation takes place only at the free hydroxy group of these dihydroxynaphthoic acids.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate.1 Publication

Kineticsi

kcat is 0.69 min(-1) with 2,7-dihydroxy-5-methyl-1-naphthoate as substrate. kcat is 0.27 min(-1) with 3,5-dihydroxy-2-naphthoate as substrate. kcat is 0.030 min(-1) with 3,7-dihydroxy-2-naphthoate as substrate. kcat is 0.0080 min(-1) 1,4-dihydroxy-2-naphthoate with as substrate.1 Publication

  1. KM=206 µM for 2,7-dihydroxy-5-methyl-1-naphthoate1 Publication
  2. KM=352 µM for 3,5-dihydroxy-2-naphthoate1 Publication
  3. KM=66 µM for 3,7-dihydroxy-2-naphthoate1 Publication
  4. KM=24 µM for 1,4-dihydroxy-2-naphthoate1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Pathwayi: Antibiotic biosynthesis

    This protein is involved in Antibiotic biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei11 – 111Substrate1 Publication
    Binding sitei133 – 1331S-adenosyl-L-methionine1 Publication
    Binding sitei153 – 1531S-adenosyl-L-methionine1 Publication
    Binding sitei177 – 1771S-adenosyl-L-methionine; via carbonyl oxygen1 Publication
    Binding sitei200 – 2001S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication
    Active sitei246 – 2461Proton acceptorPROSITE-ProRule annotation
    Binding sitei247 – 2471Substrate1 Publication

    GO - Molecular functioni

    • O-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    • antibiotic biosynthetic process 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

    BRENDAi2.1.1.303. 13527.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferaseCurated (EC:2.1.1.3031 Publication)
    Alternative name(s):
    Neocarzinostatin O-methyltransferaseCurated
    Neocarzinostatin biosynthesis protein B1Curated
    Gene namesi
    Name:ncsB11 Publication
    OrganismiStreptomyces carzinostaticus
    Taxonomic identifieri1897 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111R → A or W: Still able to methylate naphthoate. Induces a doubling of KM. 1 Publication
    Mutagenesisi11 – 111R → K: Increased ability to methylate naphthoate. Increased rate of turnover. 1 Publication
    Mutagenesisi293 – 2931Y → I: Still able to methylate naphthoate. Induces an increase of KM. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3323322,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferasePRO_0000430701Add
    BLAST

    Structurei

    Secondary structure

    1
    332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 134Combined sources
    Helixi17 – 2812Combined sources
    Helixi30 – 356Combined sources
    Helixi41 – 488Combined sources
    Helixi52 – 6413Combined sources
    Beta strandi67 – 704Combined sources
    Beta strandi74 – 785Combined sources
    Helixi82 – 854Combined sources
    Beta strandi89 – 913Combined sources
    Helixi94 – 974Combined sources
    Helixi102 – 1065Combined sources
    Helixi107 – 1126Combined sources
    Helixi113 – 1197Combined sources
    Helixi124 – 1285Combined sources
    Helixi132 – 1387Combined sources
    Helixi140 – 15819Combined sources
    Helixi161 – 1633Combined sources
    Helixi168 – 1703Combined sources
    Beta strandi171 – 1766Combined sources
    Helixi182 – 1909Combined sources
    Beta strandi195 – 2006Combined sources
    Helixi202 – 21413Combined sources
    Turni218 – 2203Combined sources
    Beta strandi221 – 2255Combined sources
    Beta strandi237 – 2437Combined sources
    Helixi245 – 2473Combined sources
    Helixi250 – 26415Combined sources
    Turni265 – 2673Combined sources
    Beta strandi269 – 2746Combined sources
    Helixi284 – 29411Combined sources
    Helixi301 – 31010Combined sources
    Beta strandi313 – 3208Combined sources
    Beta strandi322 – 33110Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3I53X-ray2.08A/B1-332[»]
    3I58X-ray2.69A/B1-332[»]
    3I5UX-ray2.60A/B1-332[»]
    3I64X-ray3.00A/B1-332[»]
    ProteinModelPortaliQ84HC8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ84HC8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 1795S-adenosyl-L-methionine binding1 Publication
    Regioni227 – 2282S-adenosyl-L-methionine binding1 Publication
    Regioni242 – 2432S-adenosyl-L-methionine binding1 Publication

    Sequence similaritiesi

    Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.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.

    Q84HC8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGKRAAHIGL RALADLATPM AVRVAATLRV ADHIAAGHRT AAEIASAAGA
    60 70 80 90 100
    HADSLDRLLR HLVAVGLFTR DGQGVYGLTE FGEQLRDDHA AGKRKWLDMN
    110 120 130 140 150
    SAVGRGDLGF VELAHSIRTG QPAYPVRYGT SFWEDLGSDP VLSASFDTLM
    160 170 180 190 200
    SHHLELDYTG IAAKYDWAAL GHVVDVGGGS GGLLSALLTA HEDLSGTVLD
    210 220 230 240 250
    LQGPASAAHR RFLDTGLSGR AQVVVGSFFD PLPAGAGGYV LSAVLHDWDD
    260 270 280 290 300
    LSAVAILRRC AEAAGSGGVV LVIEAVAGDE HAGTGMDLRM LTYFGGKERS
    310 320 330
    LAELGELAAQ AGLAVRAAHP ISYVSIVEMT AL
    Length:332
    Mass (Da):34,592
    Last modified:June 1, 2003 - v1
    Checksum:iB3DF01BE1EE9D65C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY117439 Genomic DNA. Translation: AAM77984.1.

    Genome annotation databases

    KEGGiag:AAM77984.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY117439 Genomic DNA. Translation: AAM77984.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3I53X-ray2.08A/B1-332[»]
    3I58X-ray2.69A/B1-332[»]
    3I5UX-ray2.60A/B1-332[»]
    3I64X-ray3.00A/B1-332[»]
    ProteinModelPortaliQ84HC8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAM77984.

    Enzyme and pathway databases

    BRENDAi2.1.1.303. 13527.

    Miscellaneous databases

    EvolutionaryTraceiQ84HC8.

    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 nameiNCSB1_STRCZ
    AccessioniPrimary (citable) accession number: Q84HC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: June 1, 2003
    Last modified: April 13, 2016
    This is version 56 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. 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.