ID A0A061H1J2_9BASI Unreviewed; 598 AA.
AC A0A061H1J2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=PFL1_05804 {ECO:0000313|EMBL:EPQ26482.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ26482.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ26482.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ26482.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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DR EMBL; KE361644; EPQ26482.1; -; Genomic_DNA.
DR RefSeq; XP_007881533.1; XM_007883342.1.
DR AlphaFoldDB; A0A061H1J2; -.
DR GeneID; 19319889; -.
DR KEGG; pfp:PFL1_05804; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_6_0_1; -.
DR OrthoDB; 2079054at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR038732; HpyO/CreE_NAD-binding.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF13454; NAD_binding_9; 1.
DR Pfam; PF13738; Pyr_redox_3; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 4: Predicted;
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:UP000053664}.
FT DOMAIN 21..158
FT /note="FAD-dependent urate hydroxylase HpyO/Asp
FT monooxygenase CreE-like FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF13454"
FT REGION 179..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 66913 MW; FD5BDD6F9FBF0117 CRC64;
MSSPYAANGA AAGAVGQRIL VVGGGAAGLV TLRNLLDVKT PSGQPAFDVT LVERRDDVGG
VWYWSDETYQ LERSLSPDRT QSVWPLKDQS GRPHWPSPAY LNLKGNVLPE YLQFAGHPFP
PPSHGDTFPT LKETHDYLRS FAKPLESHIR LGIEVLRVEE LLQGGWEVEW KDWNRSADRQ
ADRASSSSAP LQQTSGPSQE TTVQRFDRVV VACGWYDTPL YPKAEGMAEA RRAGFVHHAK
HYRDSATYRG KKVVVVGNNN SSNEAAAHLA VHNTREQPVY KSAKRPPVVK CPCLPDERIR
DVGVIARYEL VPQETGSPRL RVHIEDGTVI EDVDYVLLGT GYGHSFPFVR VLTDEARTAQ
RQQTQKLTPP ELQGVRVPNL FRHILFAKSA DLSLAFVGVV VSFFPFNMAD LSSRWLSLVW
SGRIRSAVPA SVEERLKDEQ DRLEYIWTDK ERHLAARNGG RPAATLDRSD PMNAFGFHTL
GGSLKEGGPS ELVYGAQLRR EIVEADPSMA DWYDDWGEER ERKQYEMYDI KRRWLLDNEE
RIKSDPFDLL GRNSAYRHLA DEMVAQQSGA EQVVDDRTTA AAPPAPVAPM PSMRKVAV
//
