ID   AZIB2_STREG             Reviewed;         345 AA.
AC   B4XY98;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase {ECO:0000305};
DE            EC=2.1.1.302 {ECO:0000269|PubMed:20485749};
DE   AltName: Full=Azinomycin biosynthesis protein B2 {ECO:0000305};
GN   Name=aziB2 {ECO:0000303|PubMed:18635006};
GN   Synonyms=azi5 {ECO:0000312|EMBL:ABY83144.1};
OS   Streptomyces sahachiroi.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=285525;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 33158 / NBRC 13928 / NRRL 2485;
RX   PubMed=18635006; DOI=10.1016/j.chembiol.2008.05.021;
RA   Zhao Q., He Q., Ding W., Tang M., Kang Q., Yu Y., Deng W., Zhang Q.,
RA   Fang J., Tang G., Liu W.;
RT   "Characterization of the azinomycin B biosynthetic gene cluster revealing a
RT   different iterative type I polyketide synthase for naphthoate
RT   biosynthesis.";
RL   Chem. Biol. 15:693-705(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RC   STRAIN=ATCC 33158 / NBRC 13928 / NRRL 2485;
RX   PubMed=20485749; DOI=10.1039/b926358f;
RA   Ding W., Deng W., Tang M., Zhang Q., Tang G., Bi Y., Liu W.;
RT   "Biosynthesis of 3-methoxy-5-methyl naphthoic acid and its incorporation
RT   into the antitumor antibiotic azinomycin B.";
RL   Mol. Biosyst. 6:1071-1081(2010).
CC   -!- FUNCTION: O-methyltransferase that mediates the formation of 3-methoxy-
CC       5-methyl-1-naphthoate from 3-hydroxy-5-methyl-1-naphthoate in the
CC       biosynthesis of the antitumor antibiotic azinomycin B.
CC       {ECO:0000269|PubMed:20485749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-5-methyl-1-naphthoate + S-adenosyl-L-methionine = 3-
CC         methoxy-5-methyl-1-naphthoate + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:18577, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:78252, ChEBI:CHEBI:78620;
CC         EC=2.1.1.302; Evidence={ECO:0000269|PubMed:20485749};
CC   -!- ACTIVITY REGULATION: Inhibited by different divalent cations, such as
CC       Mg(2+), Mn(2+), Fe(2+), Cu(2+) and Zn(2+).
CC       {ECO:0000269|PubMed:20485749}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=145 uM for 3-hydroxy-5-methyl-1-naphthoate
CC         {ECO:0000269|PubMed:20485749};
CC         KM=61 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:20485749};
CC         Note=kcat is 0.44 min(-1). {ECO:0000269|PubMed:20485749};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000303|PubMed:18635006}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; EU240558; ABY83144.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4XY98; -.
DR   SMR; B4XY98; -.
DR   KEGG; ag:ABY83144; -.
DR   GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR031725; ASMT_dimerisation.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; PTHR11746; 1.
DR   Pfam; PF16864; Dimerisation2; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..345
FT                   /note="3-hydroxy-5-methyl-1-naphthoate 3-O-
FT                   methyltransferase"
FT                   /id="PRO_0000430812"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         205
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   345 AA;  36307 MW;  BFDFE45CE8D8D0D9 CRC64;
     MAAGSGSGTP PGTPPPTLLT DLATGLWKTQ TLTAAIETGL FEALAAGDAD APETAQRLGI
     GKRPAEILLT ACTALGLLEQ RDGRYRNTAV AAHYLVPGLP DYFGGYVQMV ARYTAPGWLR
     ATEAVRTDAP TKPVPDPDRN MFEEGNRPES FWEGLFTFST LTARQLAASV DLSGVRRIMD
     VGGGAGATLI ELCRQHPHLS GTVVDLPHVC ALAGERIAAA GMTGRIDTAA ADFFADPLPS
     GHDAVLLSMI LHDWDESQNR KILASCLDAL PSGGTVLISE LLVDDDKSGP VDAALMSMNM
     LVGTWGRNYT GAEYTDWLRD AGCSEVRTVR FASPGANGVV AGVKA