ID A0A094ETX3_9PEZI Unreviewed; 366 AA.
AC A0A094ETX3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=V500_10902 {ECO:0000313|EMBL:KFY82014.1};
OS Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY82014.1, ECO:0000313|Proteomes:UP000029284};
RN [1] {ECO:0000313|EMBL:KFY82014.1, ECO:0000313|Proteomes:UP000029284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KFY82014.1}.
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DR EMBL; JPKC01003598; KFY82014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094ETX3; -.
DR STRING; 1420913.A0A094ETX3; -.
DR HOGENOM; CLU_026673_20_2_1; -.
DR Proteomes; UP000029284; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-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.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029284};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 20..366
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 366 AA; 38719 MW; C8755163F87536D8 CRC64;
MAPEPQFNGW LGRDASAAKG NMTWGPYTPK PFTSSDIDIQ ITHCGVCGSD IHTLRSGWGE
TPYPCVVGHE IIGTAIRVGS QAQKERGINV GDRVGVGAQA SSCLKADCEA CSEGEETHCP
HMVGTYGGRF PDGSKSFGGY GDFSRTPGHF VVKIPEGIES ADAAPMMCGG VTVYAPLKKN
GCGTTAKRVG IVGVGGLGHF GLLFAKALGA EKVVAISRTS AKKADAEKMG ATGFIATEDE
DWAKENAGTL DLIISTVSSP KMPLSGYLSL LAANGQFIQV GAPEDVLPPI SAFSLIMKGI
KIGGSLIGTP KDIEEMLQLV VEKKVKPWIQ KIPMTEANRA VVEFEEGKPR YRFCLVNEKN
IEKLGL
//
