ID   K1Y5N9_MARBU            Unreviewed;       506 AA.
AC   K1Y5N9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Salicylate hydroxylase {ECO:0000313|EMBL:EKD20524.1};
GN   ORFNames=MBM_01206 {ECO:0000313|EMBL:EKD20524.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20524.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD20524.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20524.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; JH921429; EKD20524.1; -; Genomic_DNA.
DR   RefSeq; XP_007289095.1; XM_007289033.1.
DR   AlphaFoldDB; K1Y5N9; -.
DR   STRING; 1072389.K1Y5N9; -.
DR   GeneID; 18757141; -.
DR   KEGG; mbe:MBM_01206; -.
DR   eggNOG; KOG2614; Eukaryota.
DR   HOGENOM; CLU_009665_19_0_1; -.
DR   InParanoid; K1Y5N9; -.
DR   OMA; RLVWYPC; -.
DR   OrthoDB; 1113861at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR13789:SF215; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT   DOMAIN          154..341
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   506 AA;  55980 MW;  7EC4742F22FDE7B8 CRC64;
     MPSSIKHSPL DIIIVGAGIA GFAAAISCRR AGHHVEIYER SALNNELGAA IHVCPNASRG
     LLAWGLDPVQ AQFVTCKRSY RAHGSTLVRF HEGDDTYVTE KFGAPWFFAH RVDLHEELKR
     LATRQDGEGR PAVVHLKSEV TRYDTAAGSV SLSSGETVFG DLVIAADGVH TGSVEAILGS
     PNPALPTTDY NFAYRFLIPT EELAADPETV QFTEDDDGRV KFFVGEGRRL VWYPCRDNKV
     HNFVAIFHSD EQVYREDWQT HVETSALLET YSAFHPSLLA VLKKAKDVKQ WPLLFRAPIS
     SWHKEKLVAI GDAAHPMLPH QGQGGAQAIE DAVALGIALS GCTPANLDRR LKVFESVRMN
     RASVMQIFSI RSRGKMLTSN ADAGQDEPEK IRTDAAKFMP AETVPKTPEE FFAYNFGYDV
     VRDSVQAMQR EDASWELPAN FFERTPVAGV YPSLEREVDV DGDSIAKSRL LDSGNGGRHL
     VTYAADVYHS VVRQVWRILK SAQYLA
//