ID A0A074XYI9_AURSE Unreviewed; 344 AA.
AC A0A074XYI9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN ORFNames=AUEXF2481DRAFT_83871 {ECO:0000313|EMBL:KEQ90540.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ90540.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ90540.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ90540.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584789; KEQ90540.1; -; Genomic_DNA.
DR RefSeq; XP_013339044.1; XM_013483590.1.
DR AlphaFoldDB; A0A074XYI9; -.
DR STRING; 1043005.A0A074XYI9; -.
DR GeneID; 25371779; -.
DR HOGENOM; CLU_026673_3_4_1; -.
DR InParanoid; A0A074XYI9; -.
DR OMA; ACITCAG; -.
DR OrthoDB; 1065708at2759; -.
DR Proteomes; UP000030641; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd08276; MDR7; 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; PTHR45033; -; 1.
DR PANTHER; PTHR45033:SF1; OXIDOREDUCTASE (EUROFUNG); 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000030641}.
FT DOMAIN 15..342
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 36861 MW; FAFC3757224061D6 CRC64;
MSLPTTARVY RRNEASNDIE QSTEELPKSL KPTEVLVQIH AVSLNFRDVA MLNNRYPAPH
SPHGIPCSDA GASVIAIGSS VTDFAVGDHV SPTFRWTTPD GVMRALGGDF EGVLRDYAVY
EADALVKNPD YLSHEEASCI PCAGVTAWTS LALDDWKKAA NIKTALMEGT GGVSLFALLI
CLGAGITPII TSSSDTKLAG LQKLAGDKKI HTINYRNIPN WAEEALKLTD GKGLDVIVNN
VGASSIEQNF AALKRFGTIS LVGFLGGTPE KMPDITTAIL HKSAHVQGIA VGTKQDHQDL
CNFLGEKKVH LGATIDKVFS FDDSPDAFKY LYSGAHVGKV VIKI
//