ID I2K3M2_DEKBR Unreviewed; 375 AA.
AC I2K3M2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Nadph-dependent medium chain alcohol dehydrogenase with broad substrate specificity {ECO:0000313|EMBL:EIF49824.1};
GN ORFNames=AWRI1499_0213 {ECO:0000313|EMBL:EIF49824.1};
OS Brettanomyces bruxellensis AWRI1499.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF49824.1, ECO:0000313|Proteomes:UP000004997};
RN [1] {ECO:0000313|EMBL:EIF49824.1, ECO:0000313|Proteomes:UP000004997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF49824.1,
RC ECO:0000313|Proteomes:UP000004997};
RX PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL PLoS ONE 7:E33840-E33840(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={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:EIF49824.1}.
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DR EMBL; AHIQ01000015; EIF49824.1; -; Genomic_DNA.
DR Proteomes; UP000004997; 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:SF39; NADP-DEPENDENT 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:UP000004997};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 21..364
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
FT UNSURE 248
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:EIF49824.1"
SQ SEQUENCE 375 AA; 41205 MW; 1A57FC0F0CE4D2F0 CRC64;
MAYPDTFEGF AVFDPSPATW STVKKFEFKP KPFEAHDVDI RINTCSICGS DVHSASNGWR
KPNAHYPLVV GHEIVGRVVR VGAAVTDFKP GDRVGVGAQA QACLKCKLCK SHNEIYCPKL
VHTFGGVYHN EDGSTTFSNG GYSNYARIND YFVFHIPPEL TDAEAAPMLC AGVTTFSPLV
RNIPKELPXG QLRPRVGIVG LGGLGMMGIQ WAHALGCETT VFSRSSRKCA DARKLGADHF
IATAEDKDWV RKVEFSLDLI ICTANSTQNF DLDTYLRALV VGGKWVNVGL PEAPFSVSPR
SFMANACFMG GSHLGSHVEM VRMFKLAVEK GVRAWTDKIP ISAQGVKEGL ERCRDHRCRY
RVALTDFDDA FPGRX
//
