ID A0A2P7YJT7_9ASCO Unreviewed; 464 AA.
AC A0A2P7YJT7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
GN ORFNames=C7M61_004070 {ECO:0000313|EMBL:PSK36248.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK36248.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK36248.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK36248.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSK36248.1}.
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DR EMBL; PYFQ01000012; PSK36248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YJT7; -.
DR STRING; 418784.A0A2P7YJT7; -.
DR EnsemblFungi; C7M61_004070_t1; PSK36248.1; C7M61_004070.
DR VEuPathDB; FungiDB:C7M61_004070; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000241107; 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; IPR023753; FAD/NAD-binding_dom.
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; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000332; FMO; 3.
DR PRINTS; PR00370; FMOXYGENASE.
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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107}.
FT DOMAIN 6..243
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 464 AA; 52717 MW; 5E4C8D0B29407F1C CRC64;
MALYRRIAII GGGPAGLAAA KALALEPYNF TIDLYERRDN IGGLWYYGGD KTKVLPSVPS
VGPDAHEILD PNGGFENRFF SPMYDQLETN IVSRLMKYNR VSGAHFTTDI KEYPGRSQVL
DYIHEYKETI PQVANFHYNK NIKKIVKNED EWSVTVEDSI SLEQETKTFD AVIIANGHFE
IPFIPDTPGL ADWAKRDPHS VIHAKYFKDG APFRDRNVIV VGALTSGIDL STQISTVAKN
TYVSVKDDPK DHDNKNEAVT MLPLITLYDY ATKTAKLVDG REISDIDDIV FCTGYLYSYP
FLKDYLPHVT DGLQVKDIYL QLFRVDDPSI AFIALPKDVV PMPLSEAQMA VVARVYSGRL
HLPDEQKRRE AYEKELSAKG AGKQFHSLKT PKDVEYCKLL YNWIQEEGLL DKGLVPSSWG
EQRLEDRKNT KADKEARLEV ILEHAAKLRK EHLVFKLPER ENER
//
