ID   A0A1C1CWC3_9EURO        Unreviewed;       381 AA.
AC   A0A1C1CWC3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Aryl-alcohol dehydrogenase {ECO:0000313|EMBL:OCT52761.1};
GN   Name=xylB {ECO:0000313|EMBL:OCT52761.1};
GN   ORFNames=CLCR_10376 {ECO:0000313|EMBL:OCT52761.1};
OS   Cladophialophora carrionii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT52761.1, ECO:0000313|Proteomes:UP000094526};
RN   [1] {ECO:0000313|Proteomes:UP000094526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA   Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA   Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL   Submitted (JUL-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|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:OCT52761.1}.
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DR   EMBL; LGRB01000008; OCT52761.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C1CWC3; -.
DR   STRING; 86049.A0A1C1CWC3; -.
DR   VEuPathDB; FungiDB:CLCR_10376; -.
DR   VEuPathDB; FungiDB:G647_04111; -.
DR   eggNOG; KOG0022; Eukaryota.
DR   Proteomes; UP000094526; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43350:SF2; PKS_ER DOMAIN-CONTAINING PROTEIN-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:UP000094526};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          25..379
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   381 AA;  40801 MW;  44129991BD6F27B9 CRC64;
     MATETQALVS YPVDTTTLKP DWRFGTVKLL RSPKEHELKI RMVATGICHS DIVVASIPNQ
     PERGLTFPKV LGHEGAGIVE EVGPGVTAAQ VGDPVLLSYS YCGDCDLCKV DQQPYCLSWM
     VLNIVGEKGH FETQAGEDTP GKFFGQSSFA GASIVGEKSV VNLKGLVSSE DELKLLAPMG
     CGLMTGSGAV INGAAVKAHD IVLVTGLGAV GMGAIMAAKI AGCREIIALD RVAHRLETAK
     ELGATKVLDT TTVPADFAEE IQKLVGGQRI SVVVETTAAV PVINESLKAL GKHGKFIQLG
     APGYGTEVTL PLQQFFNENK SFECHCLGNT TGQAWIPVMI KWWREGKFPI EKIVKYFQAK
     EAVQAIHEME NGSTIKPVLV W
//