ID A0A165CVK1_EXIGL Unreviewed; 356 AA.
AC A0A165CVK1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=NAD(P)-binding protein {ECO:0000313|EMBL:KZV83218.1};
GN ORFNames=EXIGLDRAFT_777790 {ECO:0000313|EMBL:KZV83218.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV83218.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV83218.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV83218.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV426283; KZV83218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165CVK1; -.
DR STRING; 1314781.A0A165CVK1; -.
DR InParanoid; A0A165CVK1; -.
DR OrthoDB; 179761at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05288; PGDH; 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; IPR041694; ADH_N_2.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR045010; MDR_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR43205:SF42; ALCOHOL DEHYDROGENASE, ZINC-CONTAINING (AFU_ORTHOLOGUE AFUA_7G04530); 1.
DR PANTHER; PTHR43205; PROSTAGLANDIN REDUCTASE; 1.
DR Pfam; PF16884; ADH_N_2; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 26..343
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 356 AA; 39184 MW; 252C5EEE95F7E04E CRC64;
MRRDLILMSL PPTYTRVVFA ERPVGDIVPH KTFRIEPEHK LADLEPGEKQ VLVAVDYLSL
DPAMLLWLNE NPYREPVRIG DTMDAEGLGT IVKTGKDSKW KVGQTVKGGF GWTEYAQMDD
GAVALHEVPQ GGQLLDFLGP LGNIGMTAYF GLFEIGKPKP GETLVVSGAA GAVGSLVCQL
GVLKGLKVYA IAGSDEKVQW LEKELGVTKA FNYKNKDVYD QLKEHMGTFD VFFDNVGGEM
LEFMLTRMNL HARIVICGGM SDYNNPTPSG IKGHLNLISA RALMQGFLFF DYASKFGPAV
AEMQQWLSEG KLKRKYYIVD GVKSAPEALP MLFSGGNTGK LIVRVSNIRE GVETKE
//
