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Database: UniProt
Entry: Q2USP5_ASPOR
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Original site: Q2USP5_ASPOR 
ID   Q2USP5_ASPOR            Unreviewed;       567 AA.
AC   Q2USP5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=AO090005000347 {ECO:0000313|EMBL:BAE55420.1};
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:BAE55420.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE55420.1, 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).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; AP007151; BAE55420.1; -; Genomic_DNA.
DR   RefSeq; XP_001817422.1; XM_001817370.2.
DR   AlphaFoldDB; Q2USP5; -.
DR   EnsemblFungi; BAE55420; BAE55420; AO090005000347.
DR   GeneID; 5989367; -.
DR   KEGG; aor:AO090005000347; -.
DR   VEuPathDB; FungiDB:AO090005000347; -.
DR   HOGENOM; CLU_018354_4_2_1; -.
DR   OMA; RNAISHM; -.
DR   OrthoDB; 1641938at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 2.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR13878:SF179; FAD_FMN-CONTAINING ISOAMYL ALCOHOL OXIDASE MREA (AFU_ORTHOLOGUE AFUA_6G03620); 1.
DR   PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..567
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004217413"
FT   DOMAIN          117..296
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   567 AA;  62025 MW;  83E982014D6FC70A CRC64;
     MPSLSTLKLG AFLGLAAIAP SIEAADSSSC RCFPGDDCWP SVSTWDAFNQ SVDGRLVATV
     PLATPCHTPN YDQTKCEALK EDWLLPEDHY QSSSSLMAPW FTNGTCDPYH PVSQPCTLGN
     FVRYAVNVST PAHVAKTLQF ANEHNIRFVI RNTGHDYNGK STGAGALSVW THHLKGIEFK
     DWKDEHYTGK AVKLGAGVQG FEAYEAANAQ GLRVVGGECP SVGIAGGYSQ GGGHSFLSSM
     YGLGADQVLE WEVIDGTGRL LVANRQNNTD LYWALSGGGG GTYGVVWSMT SKAYPDSQVS
     GLNLTFTTTG ISDDTFYKAV ELYNARLPSF VDQGIMSLNF MTNVSFSLSP MTAPGMPLEK
     LESLIKPFLN ELKALGIKYQ YHAESFPAYL DQFNAQAPLV EIAVAQYGSW LLPRSVVENN
     STNRELIQSY RTILSTGANF TNVGLKVSKE VAGDVDNAVN PAWRNAISHM LLYTGWEFDQ
     REKMVEAQKL MTEVLVPAFS KLAPESGAYL NEADFHQPDF KTAFFGNNYD KLRAIKAKYD
     PNDLFYALTA VGSDEWTVSE SGRMCRV
//
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