ID G7X763_ASPKW Unreviewed; 473 AA.
AC G7X763;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:GAA83085.1};
GN ORFNames=AKAW_01200 {ECO:0000313|EMBL:GAA83085.1};
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:GAA83085.1};
RN [1] {ECO:0000313|EMBL:GAA83085.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA83085.1};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; DF126448; GAA83085.1; -; Genomic_DNA.
DR AlphaFoldDB; G7X763; -.
DR VEuPathDB; FungiDB:AKAW_01200; -.
DR eggNOG; ENOG502RGYQ; Eukaryota.
DR InParanoid; G7X763; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..473
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003505316"
FT DOMAIN 55..225
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 473 AA; 51591 MW; 06BE17E6DAAEA2DE CRC64;
MKAPFTLALL LSVVGYQPWA LYLAEVCEEL GPQLSKSAVI SAWDATRYER WIKSNAPTPG
VVVTPATEQD VAAIVSYCTS NNISFLAQNG GHGWSQTIHL GEDGLLINLK QLDEVTFSKN
RREVIVGGGA SVAQVIEASS NNNALVQTNN CNCIGALGAL LGAGYGSLMG LFGFGIDNVL
SLNLVMADGC LHTITPKDID LFWALRGAGP NFGIVTSAKM KSYPVSASGQ AAWTGQLVFS
ADKLEALVDT IDRITLEPEM SVIMYFMTSG EPDNTPMVAL MLYYYGTEEK GRAAFSCFFD
LGPTNDTTMA TEYAHWVDAS SMACSKSGFK IPYSAGLSRM VSSTWKEAWE EYVSFVSLGG
TGQSIVLLEA YSLDKARFFG QDSSAYAWRT KVNFNAMAIA WYMDDSLESN ARKWASKMRD
LWRSTDGLDS PAVYINFAFD EDLSVVYGDN VDGLKAIKAK YDPENVFNQW FSL
//
