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Database: UniProt
Entry: A0A094AWW1_9PEZI
LinkDB: A0A094AWW1_9PEZI
Original site: A0A094AWW1_9PEZI 
ID   A0A094AWW1_9PEZI        Unreviewed;       893 AA.
AC   A0A094AWW1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=V491_00822 {ECO:0000313|EMBL:KFY27625.1};
OS   Pseudogymnoascus sp. VKM F-3775.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY27625.1, ECO:0000313|Proteomes:UP000029338};
RN   [1] {ECO:0000313|EMBL:KFY27625.1, ECO:0000313|Proteomes:UP000029338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY27625.1,
RC   ECO:0000313|Proteomes:UP000029338};
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617}.
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:KFY27625.1}.
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DR   EMBL; JPJT01000409; KFY27625.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AWW1; -.
DR   HOGENOM; CLU_323683_0_0_1; -.
DR   Proteomes; UP000029338; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   CDD; cd11063; CYP52; 1.
DR   CDD; cd08249; enoyl_reductase_like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002974; Cyt_P450_E_CYP52_ascomycetes.
DR   InterPro; IPR047146; Cyt_P450_E_CYP52_fungi.
DR   InterPro; IPR036396; Cyt_P450_sf.
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; PTHR24287; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR24287:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR01239; EP450IICYP52.
DR   PRINTS; PR00385; P450.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029338}.
FT   DOMAIN          19..341
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   893 AA;  97731 MW;  77F227DA8472EC2C CRC64;
     MPGIIVSNGI PASQTAIIAN ETGEFIVAHD VPVMDLEPGT IIIKTAAVAL NPVDTKMIGD
     FSTPGAILGN DCAGTIVAID PQVKAPLKIG DRVCGSADGM NRLRPSGGAF AEYVSCLGDL
     VMKIPDDMSF EEAAPIGTAV ASAVLSVFYS AKVPGTLAKP TKAPQWVLVN GGSSSTGTMA
     LQLIKLAGFR PIATCSPKNF ALAKSYGAEK VFDYRSATCA QDIREYTKNT LEFIIDCITV
     EATMKLCYQA MGRAGGNYTA LEPPPEAQHT RKAIKHDWIL ATATTGRSCS WPEPYGRPGD
     PLIRAFAEDF AVQTQVVFSE GKLKPHPARV LKVCSMGRGV VDREDRDSEL PSTEARAVGH
     NIGINSTDYS TRGQAPNLNI LTDLYTPMPP NSAWPAGDIR AARAAQANMK ALAPEVKRWT
     CFRQALRSLL PFSLEAKYKV LRFKGDFLED WVTQRFRQHG CWTYANDSRL DPSIFTAEPA
     LIQAVLATHF SDWGLGASRA NAVGPLLGPG VFTSDGPIWQ HSRAVLRPQF ARDLISDLKH
     TQRHVQQLFK AMPLGDDGWT QTTDLLPLIL RFTLDVSTQY FVGESMESQS KDNSVLERAF
     KDANAGVQLR LKVGPFVRLA STKSFREACR TWAEYGTHFV EHAARLRDTS GSSPEEEKER
     AKYSFLRGLA ASTDNNTTLM RDLTIQLLFA GEDTSASLLS FTLRCLAHHA GSYAHLRAEV
     IAKFGTKSTP AAPITFTSLK ECEHLQNVLK ETLRLYPPIP FNTREALKDT VLPVGGGKDG
     KSPCVVAKGT VVKYSVYVMQ RRMDLWGSDA TQWKPDRWVG RRAGWEYLPF NGGPRICMGQ
     QFALTEAAYA LVRICQNYDS IECTMPEDEI STRFATALFP KLGVPIRMHW ASA
//
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