ID A0A0D7ANZ6_9AGAR Unreviewed; 531 AA.
AC A0A0D7ANZ6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Putative halogenase {ECO:0000313|EMBL:KIY53484.1};
GN ORFNames=FISHEDRAFT_63324 {ECO:0000313|EMBL:KIY53484.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY53484.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY53484.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY53484.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN881616; KIY53484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7ANZ6; -.
DR OrthoDB; 1599601at2759; -.
DR Proteomes; UP000054144; Unassembled WGS sequence.
DR GO; GO:0140907; F:flavin-dependent halogenase activity; IEA:UniProt.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
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; PTHR43747; FAD-BINDING PROTEIN; 1.
DR PANTHER; PTHR43747:SF1; FAD_BINDING_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
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:UP000054144}.
FT DOMAIN 29..370
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 531 AA; 58756 MW; 62A9FF5456BF0673 CRC64;
MAEERLQTLK ETAVPVEPDV QPHQLPDSTT ICVIGGGPAG SYAACALARE GFDVVLLERY
HFPRYHIGES MLPSCRAFLR FIGAEEKVKA HGFTHKPGAA VKLNQYKREG YTDFVSLNPD
NGAWNVIRSE FDELLLRHAS DCGVKVFEGV SAESIRFDAS DPTRPVAVTW SSDRGVSGIL
RFDWLVDASG RRGIMATKHL KSRKFTKSLQ NIALWGYWTG GRKYAPGTTR ENAPWFEALT
DETGWAWFIP LHDGTTSVGI VLNAESHKVK KSGDNDVHCY LQQLKLAPGV GRFLISATFE
GEVRTAGDYS YSSTQYSGNR FRLVGDAAAF IDPFFSSGVH LAFTSALSAA ASIAASIRDQ
CSEADAAGYH NSKVGTSYTR FLIVVLGIYK QIRAQSAAVL HDVDEDNFDK AFHFLRPVIQ
GCADTDPLLT EQELQGTMDF CKNVFAPTQP EMYRSVASRY PAALMNSASP TVSIREVERV
TQGDEDAKHV LLEINARKPI HVMYDVQHFR TEILDGYFIN MEKGKLGMVR A
//