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Database: UniProt
Entry: A0A0F0ILM5_ASPPU
LinkDB: A0A0F0ILM5_ASPPU
Original site: A0A0F0ILM5_ASPPU 
ID   A0A0F0ILM5_ASPPU        Unreviewed;       319 AA.
AC   A0A0F0ILM5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Short chain dehydrogenase {ECO:0000313|EMBL:KJK68036.1};
GN   ORFNames=P875_00108714 {ECO:0000313|EMBL:KJK68036.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK68036.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK68036.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJK68036.1}.
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DR   EMBL; JZEE01000149; KJK68036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0ILM5; -.
DR   STRING; 1403190.A0A0F0ILM5; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; PTHR44229; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   PANTHER; PTHR44229:SF4; 15-HYDROXYPROSTAGLANDIN DEHYDROGENASE [NAD(+)]; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
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:UP000033540}.
SQ   SEQUENCE   319 AA;  34758 MW;  3BEBACA448216638 CRC64;
     MSFSVEGRSA IVTGAGSGIN FAFAKLLLEN GCNVLIADLA LRPEARDLVE KYSTSSSAPR
     VVFQRTDVTE WKQLELMFEV AEKEFGEIDV VCPGAGVYEP HWSNFWRPPG TPESRDPQHG
     NRYALLDINL THPIRTTQLA LAHFVRRRTS GRPKHIVHIS SIAGQNPALA APIYVATKHA
     INGLVRSLGK LDSKFGIRVT AVAPGVIKTP LWTDHPEKLK IVDTANDEWV TPEEVAQVML
     ALIQQDQVSE IIGDRTGQGP QFPVRGGTVL EVSKTVRSVS AINDPGPGTR AGNTVSDMNV
     LEDEVFGLLS QKGWGTPKL
//
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