ID   K9GCM9_PEND2            Unreviewed;       350 AA.
AC   K9GCM9;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE            EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN   ORFNames=PDIG_06550 {ECO:0000313|EMBL:EKV18882.1};
OS   Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV18882.1, ECO:0000313|Proteomes:UP000009882};
RN   [1] {ECO:0000313|Proteomes:UP000009882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
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}.
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:EKV18882.1}.
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DR   EMBL; AKCT01000030; EKV18882.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9GCM9; -.
DR   STRING; 1170229.K9GCM9; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_1_1; -.
DR   InParanoid; K9GCM9; -.
DR   OMA; GPWGCGT; -.
DR   OrthoDB; 5295198at2759; -.
DR   Proteomes; UP000009882; 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:UP000009882};
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;  37100 MW;  C6837556F1D0BF61 CRC64;
     MSIPETQWAQ VAEKVGGPLV LKQIPVPKPG PDQILVKIRY SGVCHTDFHA IMGHWPIPVK
     MPLVGGHEGA GVVVAKGELV STFEIGDHAG IKWLNGSCSE CEFCRQSDTP LCANAQLSGY
     TVDGTFQQYA LGKATHASKI PKGVPLDAAA PVLCAGITVY KGLKESGVRP GQTVAIVGAG
     GGLGSLAQQY AKAMGLRVIA IDGGDEKRQM CEQLGTEVYV DFAKSKDLVA DVKAATPGGL
     GAHAVILLAV SEKPFQQASE YVRSRGTIVA IGLPPDAFLK APVFNTVIRM INIKGSYVGN
     QQDGVEALDF FARGLIKAPY KLAPLKDLPK IFELMEQGKI AGRYVIELPE
//