ID   A0A0D7A1V8_9AGAR        Unreviewed;       360 AA.
AC   A0A0D7A1V8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=GroES-like protein {ECO:0000313|EMBL:KIY45012.1};
GN   ORFNames=FISHEDRAFT_61511 {ECO:0000313|EMBL:KIY45012.1};
OS   Fistulina hepatica ATCC 64428.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX   NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY45012.1, ECO:0000313|Proteomes:UP000054144};
RN   [1] {ECO:0000313|EMBL:KIY45012.1, ECO:0000313|Proteomes:UP000054144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY45012.1,
RC   ECO:0000313|Proteomes:UP000054144};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
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   ---------------------------------------------------------------------------
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; KN882063; KIY45012.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7A1V8; -.
DR   OrthoDB; 5295198at2759; -.
DR   Proteomes; UP000054144; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08297; CAD3; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF3; ALCOHOL DEHYDROGENASE 1-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT   DOMAIN          20..356
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   360 AA;  37745 MW;  2BCA38BBD1C7D6B9 CRC64;
     MSNYAIPKTM KAAVVVPGAH AADNLQIKDV PVKPQAQLAP GECLLKMICT GVCHTDLHAA
     LGDWPVPPHS PLIGGHEGVG IVVAIGNNTA GSPVKLGDRV GVKWLANSCL NCESCRKGLE
     QTCEKAELSG YTVDGTFSEY VVSYVNHVTP IPDGFDSFAA ASILCAGVTV YRAIKYSQTA
     PGDWIVLPGA GGGLGHMAVQ YAKFMGLRPI AIDTGAEKKK LCLELGAEAW IDFRETKDIV
     AAVKAITGGK GAHSAVVTTA SSSGYTQAVD YLRTGGTLMA VGLPGTAKLE ASIFWTVFKS
     ISILGSYVGN RQDAFEAIDI AARGGVTCHY VKKGLSALKD TYIQMQAGTL AGRIVLDFKE
//