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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Binding sitei11Substrate1 Publication1
    Binding sitei133S-adenosyl-L-methionine1 Publication1
    Binding sitei153S-adenosyl-L-methionine1 Publication1
    Binding sitei177S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
    Binding sitei200S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
    Active sitei246Proton acceptorPROSITE-ProRule annotation1
    Binding sitei247Substrate1 Publication1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi11R → A or W: Still able to methylate naphthoate. Induces a doubling of KM. 1 Publication1
    Mutagenesisi11R → K: Increased ability to methylate naphthoate. Increased rate of turnover. 1 Publication1
    Mutagenesisi293Y → I: Still able to methylate naphthoate. Induces an increase of KM. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004307011 – 3322,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferaseAdd BLAST332

    Structurei

    Secondary structure

    1332
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi10 – 13Combined sources4
    Helixi17 – 28Combined sources12
    Helixi30 – 35Combined sources6
    Helixi41 – 48Combined sources8
    Helixi52 – 64Combined sources13
    Beta strandi67 – 70Combined sources4
    Beta strandi74 – 78Combined sources5
    Helixi82 – 85Combined sources4
    Beta strandi89 – 91Combined sources3
    Helixi94 – 97Combined sources4
    Helixi102 – 106Combined sources5
    Helixi107 – 112Combined sources6
    Helixi113 – 119Combined sources7
    Helixi124 – 128Combined sources5
    Helixi132 – 138Combined sources7
    Helixi140 – 158Combined sources19
    Helixi161 – 163Combined sources3
    Helixi168 – 170Combined sources3
    Beta strandi171 – 176Combined sources6
    Helixi182 – 190Combined sources9
    Beta strandi195 – 200Combined sources6
    Helixi202 – 214Combined sources13
    Turni218 – 220Combined sources3
    Beta strandi221 – 225Combined sources5
    Beta strandi237 – 243Combined sources7
    Helixi245 – 247Combined sources3
    Helixi250 – 264Combined sources15
    Turni265 – 267Combined sources3
    Beta strandi269 – 274Combined sources6
    Helixi284 – 294Combined sources11
    Helixi301 – 310Combined sources10
    Beta strandi313 – 320Combined sources8
    Beta strandi322 – 331Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3I53X-ray2.08A/B1-332[»]
    3I58X-ray2.69A/B1-332[»]
    3I5UX-ray2.60A/B1-332[»]
    3I64X-ray3.00A/B1-332[»]
    ProteinModelPortaliQ84HC8.
    SMRiQ84HC8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ84HC8.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni175 – 179S-adenosyl-L-methionine binding1 Publication5
    Regioni227 – 228S-adenosyl-L-methionine binding1 Publication2
    Regioni242 – 243S-adenosyl-L-methionine binding1 Publication2

    Sequence similaritiesi

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

    Phylogenomic databases

    KOiK20421.

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3I53X-ray2.08A/B1-332[»]
    3I58X-ray2.69A/B1-332[»]
    3I5UX-ray2.60A/B1-332[»]
    3I64X-ray3.00A/B1-332[»]
    ProteinModelPortaliQ84HC8.
    SMRiQ84HC8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAM77984.

    Phylogenomic databases

    KOiK20421.

    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: November 2, 2016
    This is version 58 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.