ID A0A0D2CYI9_9EURO Unreviewed; 357 AA.
AC A0A0D2CYI9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=PV07_08292 {ECO:0000313|EMBL:KIW28649.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW28649.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW28649.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW28649.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
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; KN847043; KIW28649.1; -; Genomic_DNA.
DR RefSeq; XP_016248865.1; XM_016395446.1.
DR AlphaFoldDB; A0A0D2CYI9; -.
DR STRING; 569365.A0A0D2CYI9; -.
DR GeneID; 27347486; -.
DR VEuPathDB; FungiDB:PV07_08292; -.
DR HOGENOM; CLU_026673_20_1_1; -.
DR OrthoDB; 5295198at2759; -.
DR Proteomes; UP000054466; 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:UP000054466};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 19..351
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 357 AA; 38272 MW; F96A0C4696E9459E CRC64;
MTSYKIPTEQ WAQVIDKVGG PVQYKKIPVP KPGPEDVLVN IKYSGVCHTD LHAVNGDWPL
PTKLPLVGGH EGAGIVVARG ELVTDDICKI GEAVGVKWLN DSCLNCTFCQ QSDEPLCLTP
KLSGYTVDGS FQQYCVASAR HVAHIPDGVP LDEVSPVLCA GITVYKGLKE SGARPGQTVA
IVGAGGGLGS LAQQYARAMG IHTIAIDTGD DKKALCEKMG SSTFIDFAKS SDVVKDVKAA
TKDGLGPHAV ILVAVTEKPF QQAAEYVRPR GTVIVIGLPA KAYIRAPVFE SVVKMIRIQA
SYVGNRQDSE EALDFFARGL IKVPFKTVDL KDLPKVYEMM HAGQIAGRYV LKMPDPE
//
