ID A0A1E3PB17_WICAA Unreviewed; 498 AA.
AC A0A1E3PB17;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=WICANDRAFT_82601 {ECO:0000313|EMBL:ODQ62609.1};
OS Wickerhamomyces anomalus (strain ATCC 58044 / CBS 1984 / NCYC 433 / NRRL
OS Y-366-8) (Yeast) (Hansenula anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=683960 {ECO:0000313|EMBL:ODQ62609.1, ECO:0000313|Proteomes:UP000094112};
RN [1] {ECO:0000313|EMBL:ODQ62609.1, ECO:0000313|Proteomes:UP000094112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58044 / CBS 1984 / NCYC 433 / NRRL Y-366-8
RC {ECO:0000313|Proteomes:UP000094112};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KV454208; ODQ62609.1; -; Genomic_DNA.
DR RefSeq; XP_019041816.1; XM_019185407.1.
DR AlphaFoldDB; A0A1E3PB17; -.
DR STRING; 683960.A0A1E3PB17; -.
DR GeneID; 30202653; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000094112; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 3.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000094112}.
SQ SEQUENCE 498 AA; 56029 MW; 4E14BB72DE39AA94 CRC64;
MTIDKFNINS IAVIGGGPSG IASVYEFLHT TKDGKSTVGG SNAENPAFTK VVGFEQKNKV
GGSWAPSIEV PDLPEDELWG RNYYDADVIH PKVEIPKGLS NHSVESPLVT DGVNNDNQWR
RSAVYPGLYT NVPRRFLRFS SIKYTPPSKL AEIDPLISYK EVGQVLDKFV DDNKLLDHFR
LNTQVQDVQK DEEGKWLLTL RHSTPEGKDE WYTEKFDAVV IASGHYSVPF IPYIEGLNSA
PKGTIVHSKS FRTVDQFKDK NVLVVGSSLS GIDIIQYIEP VVKSLTISRT PGKQEIFPWI
TKAATSFSNK PRISKIDGKT VFFEDGSKLE DVDKILFATG YHWHYPYIGE KFLELTKPGY
ANKATGGSRV KGLYRDTFNI EDPTLAFIGV QITSVQFHSF EAGAVGIAGV WSNSKRLPSK
DAQKEWETKR LVETSDDYIF HYYPWDIVQK EFIDVLLEYA PDDRPYILEG EDFGDYPKAL
EAAERAFYDI KAGKYSLD
//
