ID   A0A0F0IAR0_ASPPU        Unreviewed;       365 AA.
AC   A0A0F0IAR0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Zinc-binding dehydrogenase {ECO:0000313|EMBL:KJK64181.1};
GN   ORFNames=P875_00138389 {ECO:0000313|EMBL:KJK64181.1};
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:KJK64181.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK64181.1, 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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:KJK64181.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JZEE01000519; KJK64181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IAR0; -.
DR   STRING; 1403190.A0A0F0IAR0; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08233; butanediol_DH_like; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          10..353
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   365 AA;  39246 MW;  5BCC75041210F088 CRC64;
     MKAARFYAAG DIRIEEVETP EASEDKALVQ VEWCGICGSD VNEYVQGPMS IPHTRTGPHP
     LTGDILPVTL GHELSGRIIQ APSTSSFTPG QAVIIDPRYY CSSCTACTSS VTNCCQSLGF
     LGLSGGGGGF SEKIAVPPAM LHPIPDNTDM ATATLIEPLA VAWHAVRCSG VKDFKSLPIL
     VIGGGPVGVA TVFVLRAWGA DQIYISETAR RRREFLKDLV QATFDPIDVH VGSECRSLTN
     GSGIGLVFDC AGSQKGLEAA CDALRFHGLY VNLAVPKSAI SLPPMYFMRK ELTYKSFLAY
     DDADFKATVA AFTEGKFAGV ERMITRRIAL EELVEKGFKT LLQNPDEHIK IVAAARALPS
     SDWTL
//