ID A0A0F0I456_ASPPU Unreviewed; 559 AA.
AC A0A0F0I456;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Alcohol dehydrogenase GroES-like domain protein {ECO:0000313|EMBL:KJK61946.1};
GN ORFNames=P875_00086532 {ECO:0000313|EMBL:KJK61946.1};
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:KJK61946.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK61946.1, 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 -!- 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:KJK61946.1}.
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DR EMBL; JZEE01000654; KJK61946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0I456; -.
DR STRING; 1403190.A0A0F0I456; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd08243; quinone_oxidoreductase_like_1; 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; 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; PTHR44154; QUINONE OXIDOREDUCTASE; 1.
DR PANTHER; PTHR44154:SF1; QUINONE OXIDOREDUCTASE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT DOMAIN 216..526
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 62068 MW; 8D32341AB2D53EA5 CRC64;
MASSAENSPF PGPESSNEPT PQLNIPPDIL RLRAEIFALE APITVSVTEF NNAWKYLDNI
YVRNQARYGQ KKTTTYYWCR LWRTKAYEPS VSDEQRKRKR TVREPIGCPC RIRIVSDGYY
MTITRGKEPH NHDISALDYK LTTAARELAA QAVAKGSRPS LVARELKNSG IGGQITSKDA
WNAGNVWVSR KEGRPAWQKH YPKNSVMEAI VANEPGPPDV LHVETYPRPP PKSGEILIEV
KAFGLSRSDI LARQGHTADA KFPQIMGREA VGIVTAGEGT VTPGTRVIAM ITDLLPEYPG
SYAQYTRVPA THVRRVHPLC KLSWEHLAVF SEMIPTAWNA LFRALRLHPD DRLLIRGGTT
SIGLAAACIA KRHCSFIAST TRQESRKELL EGVGVHKILI DDGSVSQQIK SEGLEFTKVL
DLIGAKTIAD SLQCVRPYGI VCQAGAIGGD STISDFNPMD AVPSTVSFTT YKSSAEDFIN
FPLDVLCHEV ETGHLKLPNI RIYFSNQIVQ AHRSIEENRA EGKVVVLWKP YNLLNYGAVL
PFEEFELLAS RPQILISPV
//