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Database: UniProt
Entry: A0A1V6QXT8_9EURO
LinkDB: A0A1V6QXT8_9EURO
Original site: A0A1V6QXT8_9EURO 
ID   A0A1V6QXT8_9EURO        Unreviewed;       843 AA.
AC   A0A1V6QXT8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=PENSOL_c030G07853 {ECO:0000313|EMBL:OQD93816.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD93816.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:OQD93816.1}.
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DR   EMBL; MDYO01000030; OQD93816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QXT8; -.
DR   STRING; 60172.A0A1V6QXT8; -.
DR   OrthoDB; 2315072at2759; -.
DR   Proteomes; UP000191612; Unassembled WGS sequence.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   CDD; cd08249; enoyl_reductase_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   InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR   PANTHER; PTHR45348; HYPOTHETICAL OXIDOREDUCTASE (EUROFUNG); 1.
DR   PANTHER; PTHR45348:SF1; TRANS-ENOYL REDUCTASE STHE; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT   DOMAIN          20..338
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   REGION          375..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   843 AA;  90194 MW;  437BF919B1EE2ED0 CRC64;
     MTFVESPQLP QFQTAVVAQG PGKLGIQHNV PIPTLTSDMA LVKTAAVAIN PADAKMLDYS
     AAPGAIHGYD FAGTVVALGE NVRAGLAVGD RVAGFVHGMN CLQPEIGAFA EYVGATADLL
     LKIPDSLSFE EAATLGVGMG TAAFGLFHEL RIPASLEQLT KANGDASKGE FVLVAGGSTA
     TGTRAIQLLK LAGLRPIATC SPAHFDLALK FGADKVFDYH SADCASDIRA YTKGQLAYAL
     DCVSLADTTE LCYKAIGRAG GRYVSLEPFR AAVTQTRPTV EPSWLMVLSL FGHEVALDGD
     YGRPARPEYR QFGAEAFAAV QALVDRGLID THPTKIMAGG WGGGSSSTTG VCDRCLRQGA
     PCVYSFSLPK GRRSTYAGNA APSDSATSRS AIANPRCTPT YSPIPAPELP AETSSEPVSA
     ARTPLLPIPE HLNINACPSF LQLEEPGHEA LRSMAWLENV EFGLGAMGTS TAHGTGASET
     QDHTGFDAFL NGTDFEDVHM SDIENMSAWS EQESLKEVYL RHGMPTDQKP VSPPPSQDLG
     HPLRQALENP TPPEDTRYNI DLVCIDDGIA QLSQLSSHLY TLCRASHDLT ANIGPCGPES
     RRLPLFDDKA LISAITWLAA PNMNINTYPP RPPSFALTGS PSGPLATSTT PENTLINTFS
     ASHYLLQVLH QLQTLPIPTT RAPPYPDLDE DVGSQTTSRL RSPSLSSTTT NSSSGMRDSA
     GSQHSSTVIR HLIIACYTLV LKMWSVLLVA LQHDAELSTE STSFLNSDKL DKEGDEDTPR
     PPLLANMRLV LVVNLSSYLV DRLRNAMHTY LSSKITGSAD HGLSELESEF RQPLRRLRRT
     LNS
//
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