ID Q2U0M8_ASPOR Unreviewed; 262 AA.
AC Q2U0M8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Dehydrogenase with different specificitie {ECO:0008006|Google:ProtNLM};
GN ORFNames=AO090011000374 {ECO:0000313|EMBL:BAE64887.1};
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:BAE64887.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE64887.1, 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 short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; AP007171; BAE64887.1; -; Genomic_DNA.
DR RefSeq; XP_001826020.1; XM_001825968.1.
DR AlphaFoldDB; Q2U0M8; -.
DR STRING; 510516.Q2U0M8; -.
DR EnsemblFungi; BAE64887; BAE64887; AO090011000374.
DR GeneID; 5998123; -.
DR KEGG; aor:AO090011000374; -.
DR VEuPathDB; FungiDB:AO090011000374; -.
DR HOGENOM; CLU_010194_1_1_1; -.
DR OMA; LFGVQCD; -.
DR OrthoDB; 1061116at2759; -.
DR Proteomes; UP000006564; Chromosome 7.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR42760:SF5; 3-DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G14350)-RELATED; 1.
DR PANTHER; PTHR42760; SHORT-CHAIN DEHYDROGENASES/REDUCTASES FAMILY MEMBER; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564}.
SQ SEQUENCE 262 AA; 27835 MW; 18610824D6DBDC11 CRC64;
MSASLFSLSG KTAIVTGGTR GIGQAMAFAL AEAGADIVLI QRDESNTSTR DEIISRIGRK
AWIHVAELSS RDAIKGVIPA LTSQGLKPEI LLNCAGIQRR HPSEQFPDED WDEVIQVNLT
SVFTLCREFG AYLLARDASE FPTGRRGSII NVASLLSFQG GITVPAYAAS KGGISQLTKA
LSNEWVSKGI NVNAIAPGYI ATDMNTALIN DSNRNAGIMA RIPAGRWGSP DDFKGVIVFL
ASQASSYVSG EVICVDGGWM GR
//
