ID   TYLM3_STRFR             Reviewed;         423 AA.
AC   P95746;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Protein TylM3 {ECO:0000303|PubMed:15612702};
GN   Name=tylMIII {ECO:0000303|PubMed:15612702};
GN   OrderedLocusNames=SFRA_32290 {ECO:0000303|Ref.2};
OS   Streptomyces fradiae (Streptomyces roseoflavus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=T59235;
RX   PubMed=9031628; DOI=10.1016/s0378-1119(96)00595-1;
RA   Gandecha A.R., Large S.L., Cundliffe E.;
RT   "Analysis of four tylosin biosynthetic genes from the tylLM region of
RT   Streptomyces fradiae.";
RL   Gene 184:197-203(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19609;
RA   Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., Danilenko V.N.;
RT   "Genome sequence of Streptomyces fradiae ATCC 19609.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=15612702; DOI=10.1021/ja043900e;
RA   Melancon C.E. III, Takahashi H., Liu H.W.;
RT   "Characterization of tylM3/tylM2 and mydC/mycB pairs required for efficient
RT   glycosyltransfer in macrolide antibiotic biosynthesis.";
RL   J. Am. Chem. Soc. 126:16726-16727(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of the macrolide antibiotic
CC       tylosin derived from the polyketide lactone tylactone. TylM3 is
CC       required for the glycosylation of the 5-hydroxyl group of tylactone to
CC       yield 5-O-mycaminosytylactone. {ECO:0000269|PubMed:15612702,
CC       ECO:0000303|PubMed:9031628}.
CC   -!- PATHWAY: Antibiotic biosynthesis; tylosin biosynthesis.
CC       {ECO:0000303|PubMed:9031628}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: Although TylM3 shows significant similarity to cytochrome P450
CC       family, it lacks the heme-binding sites. The conservation of amino acid
CC       sequence is confined primarily to the C-terminal half of the protein.
CC       {ECO:0000305}.
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DR   EMBL; X81885; CAA57471.1; -; Genomic_DNA.
DR   EMBL; JNAD01000108; KDS83993.1; -; Genomic_DNA.
DR   RefSeq; WP_050364680.1; NZ_MCNU01000256.1.
DR   AlphaFoldDB; P95746; -.
DR   SMR; P95746; -.
DR   STRING; 1906.SFRA_32290; -.
DR   KEGG; ag:CAA57471; -.
DR   eggNOG; COG2124; Bacteria.
DR   OMA; DCERFGR; -.
DR   BioCyc; MetaCyc:MON-18409; -.
DR   UniPathway; UPA01018; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR002397; Cyt_P450_B.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR030958; P450-rel_GT_act.
DR   PRINTS; PR00359; BP450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   TIGRFAMs; TIGR04515; P450_rel_GT_act; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis.
FT   CHAIN           1..423
FT                   /note="Protein TylM3"
FT                   /id="PRO_0000430768"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  44149 MW;  771A75D6FFBD8597 CRC64;
     MNTAAGPTGT AAGGTTAPAA AHDLSRAGRR LQLTRAAQWF AGNQGDPYGM ILRAGTADPA
     PYEEEIRERG PLFHSELLGT WVTGSRHVAD AVTADDAFGA LTADGARPGV RELPLSGSAL
     DAAHGNPGGP PLPGGWPHRP PDREERDDPD RHAADLLNAA GPGQVLDLVP FARRLAARTT
     GAWLGVPAER LPRFETALTG CRRALDALLC PQLLADARAG LAAEEALRAV LGETPEARGR
     PPGAVEAARA HAVSAAEPIA VLLCNAVREL MERPAQWRAL TADPGLAGAA ITETLLWAPP
     VRLESRVARE TAVLAGRTLP AGTHLVVLAA AANRDACRNA GPAVTGFDVL RRASDGGPQP
     HGLPEDLHFR LSGPLVRRTA EAGLRALAER FPGLRPAGPA VRVRRSPVLR GLGRLPVAPY
     VPE