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Database: UniProt
Entry: A0A094FM00_9PEZI
LinkDB: A0A094FM00_9PEZI
Original site: A0A094FM00_9PEZI 
ID   A0A094FM00_9PEZI        Unreviewed;       371 AA.
AC   A0A094FM00;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=V498_05317 {ECO:0000313|EMBL:KFY91786.1};
OS   Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY91786.1, ECO:0000313|Proteomes:UP000029270};
RN   [1] {ECO:0000313|EMBL:KFY91786.1, ECO:0000313|Proteomes:UP000029270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY91786.1}.
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DR   EMBL; JPKA01001188; KFY91786.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094FM00; -.
DR   HOGENOM; CLU_026673_16_5_1; -.
DR   Proteomes; UP000029270; 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; 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:SF3; PKS_ER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08240; ADH_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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          19..361
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
FT   COILED          333..360
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   371 AA;  39915 MW;  876F5DDD5177E986 CRC64;
     MTTPTHKAVA TVAVRAPLGI IQHPTIQPRE GEVLVRVEWT ASGPLDLHQN DGGLLVEHPQ
     ALGDGVAGTV KSIGPGVQNL AIGDKVFGFC FEESHHKAQQ EFVTVPETSL GKIPAGFTMQ
     EAVTVPNNLV TAFHATTADL GLPLPWPRPA SPSPVHAKSP ILIWGGNSSC GQYLIQVLTH
     WGYKNIIATA SPINHDYLRS LGAKTVFDYR DPNVVNLILE SAGGANTDGP AVPFILDCIT
     SKYGSLEKLA KIAQKGSKVA ALLPVIVKDS SDTEAPEYSM DVPASAGWAE GVEARGVRTH
     FYQENVFFKT YLQSTIIPTL LAEGVVKPNK QRIIEGKTLL ERAQKALDTL RNKAVSGERL
     VWRISEEGAN E
//
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