ID A0A0D2A1H6_9PEZI Unreviewed; 350 AA.
AC A0A0D2A1H6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=PV09_08030 {ECO:0000313|EMBL:KIW00513.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW00513.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW00513.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW00513.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; KN847563; KIW00513.1; -; Genomic_DNA.
DR RefSeq; XP_016210382.1; XM_016361878.1.
DR AlphaFoldDB; A0A0D2A1H6; -.
DR STRING; 253628.A0A0D2A1H6; -.
DR GeneID; 27316003; -.
DR VEuPathDB; FungiDB:PV09_08030; -.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; A0A0D2A1H6; -.
DR OrthoDB; 5295198at2759; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; 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; IPR002328; ADH_Zn_CS.
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.
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:UP000053259};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 16..346
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 350 AA; 37099 MW; BA3D3A578B6FC904 CRC64;
MSIPATQMAM VIEKTGGPVQ YKEIPVQKPG PDEVLVNIKY SGVCHTDLHA VNGDWPLPTK
LPLVGGHEGA GVVVAVGNLV TDVQIGDHVG VKWLNGSCLA CEFCQTSDEP LCPKALLSGY
TVDGSFQQYA IAKAAHVARI HKDIPLDAIA PVLCAGITVY KGLKESGARP GQTVAIVGAG
GGLGSLAQQY AKAMGLRIIA IDSGEEKRKM CATLGSDAFV DFATSQNVVK DVQAATEDGL
GPHAVLLVAV NEKPFQQAAE YVRPRGTVVC IGLPAGAYLK APVFESVIRM ITIKGSYVGN
RKDTQEALDF FRRGLIKAPF KVVGLSQLQE VYDLMQKGQI AGRYVLDTSK
//
