ID A0A2C5Z1R1_9HYPO Unreviewed; 472 AA.
AC A0A2C5Z1R1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=FAD-dependent urate hydroxylase HpyO/Asp monooxygenase CreE-like FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF13454};
GN ORFNames=CDD80_3475 {ECO:0000313|EMBL:PHH73916.1};
OS Ophiocordyceps camponoti-rufipedis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2004952 {ECO:0000313|EMBL:PHH73916.1, ECO:0000313|Proteomes:UP000226431};
RN [1] {ECO:0000313|EMBL:PHH73916.1, ECO:0000313|Proteomes:UP000226431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map16 {ECO:0000313|EMBL:PHH73916.1,
RC ECO:0000313|Proteomes:UP000226431};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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:PHH73916.1}.
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DR EMBL; NJES01000309; PHH73916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5Z1R1; -.
DR STRING; 2004952.A0A2C5Z1R1; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000226431; 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 InterPro; IPR038732; HpyO/CreE_NAD-binding.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR Pfam; PF13454; NAD_binding_9; 1.
DR PIRSF; PIRSF000332; FMO; 3.
DR PRINTS; PR00370; FMOXYGENASE.
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:UP000226431}.
FT DOMAIN 15..53
FT /note="FAD-dependent urate hydroxylase HpyO/Asp
FT monooxygenase CreE-like FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF13454"
SQ SEQUENCE 472 AA; 52387 MW; BE68D4DBB8F36E74 CRC64;
MGSVSPTRFN VKQIAIIGAG PSGLATAKYL IAQHAFTHIV IFEQQQEIGG IWVPPPSGVN
PPPSRCTVPQ TNPFLPPEPP VSVAEDRPRC RKVTYHYPSA VYDKLSANTV GSLMQFSDEP
FPSSCLLFPS CDDIRDSILR YGHDVRHLIR FRQQVTSLEL LQNHGHDQWR LRTRDVVSDE
AADHLFDAVV VASGHYSVPF IPDLNNSAAF HDAHPSVIIH SREYRSPESY RDKKVVVVGN
GPSGVDIAAQ INAVSKGKTI LSVKSATAPE SLAFTGCDEA SELVEFLVDE RGVRFKDGRV
ETDVDAVIFC TGFLYSFPFL NDLQSKLITS GHGVHGLYKH LFYAQHPTLV FSALPSRSVP
WPLSECQAAV VAAVWSNQLE LPPVEEMQGW SRDLHERVGE ALQLLPPGGN HHYINELHDW
AIKASYLGKQ PPRWSESDGW QHLHMGEIRR RFHKQGARAK TWADLGIEPG PS
//