ID G7XZ23_ASPKW Unreviewed; 637 AA.
AC G7XZ23;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:GAA92208.1};
GN ORFNames=AKAW_10322 {ECO:0000313|EMBL:GAA92208.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA92208.1};
RN [1] {ECO:0000313|EMBL:GAA92208.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA92208.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; DF126489; GAA92208.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XZ23; -.
DR STRING; 1033177.G7XZ23; -.
DR VEuPathDB; FungiDB:AKAW_10322; -.
DR eggNOG; KOG3855; Eukaryota.
DR InParanoid; G7XZ23; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 3.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF15; MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G03030)-RELATED; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 42..177
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 196..415
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 449..603
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 637 AA; 71132 MW; A1A65A8AD3D761BA CRC64;
MPVFTEFASK SRDLRVLPSF ALPLPRLTPP FEPTVNDGVE RYEVLIVGAG PSGLMLELLL
ARYGLSDESL LCIDSKPSTL KSGQADGVQP RTLEVFKTLG ISDEIENEAC QMWQFAFWNT
SSDPSRIIER KSVVPEVIPP ARFRYEATIH QGRIERIMET DLLRYSKRGV QRDTKLIHVQ
LNEDDKEFPV LAEIETRGCV GLKLEGQSLD HIWGVIDLVV DTNFPDIRRR CAIHAPAGSV
MVIPRERIVT GEYLTRLYVQ VPGMASPNGD IVGAAATPIS EIDDARVRRQ KVTKEGILKQ
AADAFKPYYL RPKSEESIDW WAAYQIGQRV SPEFIVKDST GVPRVFIVGD ACHTHSPKAG
QGMNVSMMDS YNLAWKLAYH IHGLSPSSAE PDQPHPLLDT YHLERHANAQ QLIDFDRKFS
TIFSGQLDTE ESGMSHAEFV ATFNTGNGFT SGCGVEYGES MIVDRTASEG QDNPIQGDDY
LSGILRPGRR LLNVKLRRHA DGWHRDIQDD LASTGRFRIL TLTSNDLLNV QSVSARSLQD
VSALLGTFPA GIVEQIVVHP QLPREFEWDS LPGCVKEHAE MRFYNGSELE DAYEIYGVDP
HQGAMVVVRP DGYVGIVVAL GEVDRVGEYL RRCIRTQ
//
