ID Q2UBE5_ASPOR Unreviewed; 598 AA.
AC Q2UBE5;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 22-FEB-2023, entry version 73.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=AO090102000004 {ECO:0000313|EMBL:BAE61120.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE61120.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE61120.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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DR EMBL; AP007162; BAE61120.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2UBE5; -.
DR EnsemblFungi; BAE61120; BAE61120; AO090102000004.
DR HOGENOM; CLU_017006_1_0_1; -.
DR OMA; MDWIGPP; -.
DR OrthoDB; 307340at2759; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR42815; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR PANTHER; PTHR42815:SF2; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT DOMAIN 319..458
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 598 AA; 65856 MW; C528CF391AED42E7 CRC64;
MQRKLGYTNA VKDAWPTIRN IMPEQHRVFH TSKLPFIPIT TVDEDGRPWA AIVAGPTGEP
GFVHSPDSQN LSIHAHLWDG DPLLDTVNAG VDPSSALSTI AQRSLAAGLG IEFSTRRRNK
FAGTIQRVEC QSSLDYKLHL RVTQTTGHWE PQGRLPEEVV AFIRQADTVF VGSIYKSSPS
DLHKFPPHVG MNARSGLPGF IRVSPSDGRT VVVPDYSGNR FMSTLGNIET SGVVGLTIVS
FTTGDILYLT GTAKNLVGPL ALEIMTRHAA ITTVNVTGFV FVRDALPVRQ QDGTPVERSP
YSPKIKYLVE ETGAKGLDSK EHKAKLREVV QVSSDLAVFK FQVISKPGAG DLRIRPGQAI
VLDFMNWIGP PQYQHMKDTA PSSINDDRVR TWTVSSAHEE RNATGFELIM REMKGGAVTG
ALFDRLRKYR STRLGQRIVF DPPVVADIVG VTGDFFMDND KLDALWVAGG IGITPFLAML
RALAERGSAA EGDVMLVLAT REPSVMLYMM RPSLERIAST VRINITIFTH DSEFDYGNLK
SNQNICVHRD RVVPDFWRDI PRGKDVFICG PSAFGDSVAD GLRAVGFSPS QIHREGFY
//