ID A0A165C8N6_9BASI Unreviewed; 509 AA.
AC A0A165C8N6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZT50406.1};
GN ORFNames=CALCODRAFT_513305 {ECO:0000313|EMBL:KZT50406.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT50406.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT50406.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT50406.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride + FADH2 + melleolide F + O2 = 6'-chloromelleolide F +
CC FAD + H(+) + 2 H2O; Xref=Rhea:RHEA:67160, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:167712,
CC ChEBI:CHEBI:167713; Evidence={ECO:0000256|ARBA:ARBA00036433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67161;
CC Evidence={ECO:0000256|ARBA:ARBA00036433};
CC -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC {ECO:0000256|ARBA:ARBA00005706}.
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DR EMBL; KV424179; KZT50406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165C8N6; -.
DR STRING; 1353952.A0A165C8N6; -.
DR InParanoid; A0A165C8N6; -.
DR OrthoDB; 1599601at2759; -.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0140907; F:flavin-dependent halogenase activity; IEA:UniProt.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006905; Flavin_halogenase.
DR PANTHER; PTHR43747:SF1; FAD-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43747; FAD-BINDING PROTEIN; 1.
DR Pfam; PF04820; Trp_halogenase; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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:UP000076842}.
SQ SEQUENCE 509 AA; 55581 MW; B4B454D4DC5A8D98 CRC64;
MADIPKHAQI LVVGGGPGGS YAATVLAREG FDVVLLESAK FPRLISDASR YHIGESMIPS
MRFFLGLIDL EETVSKHGFL IKPGAAFKLV PDRTEGYSNF TALLGKAGTS WNFKRAEFDE
ILLRNAEKCG AKVFEQVGVS SLDFQDADTA KRPLAAHWKH TPSGSSGQIT FDYLIDASGR
TGLMSTKYLK NRRFNASLNN VACWGYWKGT GRYMPGTERD NAPLFEALHD ESGWGWFIPL
HDGTTSVGIV EDQAASVRKK REAKEAPGGA EEGLKEHYLR QLKLCPGVRE LIGEGVLVEG
GEAPTVRAAS DFSYTATSYA GDHYRLVGDA AAFIDPFFSS GVHLAFTNAL SAAVSIASSI
RGDVPEKDCA AFHDAKVSLA YTKFLVIVLS AYTQMRHQNA AILSEINESD FQRAFEIINP
VIQGRAETPT RLTPNEVKKA MDFCFPLIGL GPHMPQNGPP SPEFIAKMAP FRKWLPSLSD
FNYDVINGFN VNLEKGQLGM VPVKEGESK
//
