ID A0A0F0IFT4_ASPPU Unreviewed; 478 AA.
AC A0A0F0IFT4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:KJK66560.1};
GN ORFNames=P875_00128061 {ECO:0000313|EMBL:KJK66560.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK66560.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK66560.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KJK66560.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JZEE01000239; KJK66560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IFT4; -.
DR SMR; A0A0F0IFT4; -.
DR STRING; 1403190.A0A0F0IFT4; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR PANTHER; PTHR10961:SF48; AMINO ACID OXIDASESARCOSINE OXIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G10130)-RELATED; 1.
DR PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT DOMAIN 7..445
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 478 AA; 52753 MW; 27DB3C6B73E877B4 CRC64;
MPAPKSIIIV GSGVFGLSTA HAMSQNDKFA SSKITLIDSW NFEPSGPSAS TPNPSAANFD
TSRIIRSDYS HRIYAALARE AQQKWKAEWG ADGRYRNQSI VMIGEGHSMK QPMKALESIN
YVKHAYAQSY ERAGRNRDIV HILDSELAVW EALGLGTPDE ASNIGPRASE LRGYRNHNCG
WAESGATMAW LRQKTINSDR INIHIGQVVG LRVCSDSPSE SHVNAEPRVC GVILDDGRQL
TADLTILAAG AMTPRLLGSP TLCDVYSETV AYVQLSEMER RELVRREFPL IVNVARKIFA
IGPDNQGFLK LARFSWSGYR DVQKFAGVDV GPRPQAAPLE EDGYGTCGDI DQTKLSPDVE
STLQDYRGFL RELFQPTDGG DLGGLRNIAT RPFARVRRCW YADTVSTDFI VDYHPAYGKS
LFLATGGSDH AFKFLPVLGE RICELILQSD NGKAGPSESL QELRRLWRFP GGDSHAKL
//