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Database: UniProt
Entry: A0A0A2W4B3_BEABA
LinkDB: A0A0A2W4B3_BEABA
Original site: A0A0A2W4B3_BEABA 
ID   A0A0A2W4B3_BEABA        Unreviewed;       339 AA.
AC   A0A0A2W4B3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Putative zinc-type alcohol dehydrogenase-lik e protein YjgB {ECO:0000313|EMBL:KGQ13507.1};
GN   ORFNames=BBAD15_g690 {ECO:0000313|EMBL:KGQ13507.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13507.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ13507.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13507.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
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:KGQ13507.1}.
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DR   EMBL; ANFO01000039; KGQ13507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2W4B3; -.
DR   STRING; 1245745.A0A0A2W4B3; -.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   Proteomes; UP000030106; 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; IPR029752; D-isomer_DH_CS1.
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:SF38; ALDEHYDE REDUCTASE AHR; 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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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:UP000030106};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          13..335
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   339 AA;  36315 MW;  4012F380B7586FA6 CRC64;
     MSVIKSYAAP KAGAELELQD FDAGDLLPED VEVQVEYCGI CHSDLSMIDN EWGFSQYPLV
     AGHEVIGRVH ALGSSAKNKG LKVGQRVGIG WTARSCGHCD ACISGSQINC QQGSTATIMN
     RGGFADKIRA DWQWVIPLPD SIDIASAGPL LCGGITVFKP LLMHHITATS RVGVIGIGGL
     GHIAIKLLHA MGCEVTAFSS NPAKKEEVLA MGADKVVNSR DPAELTALAG QFDLIINTVN
     VDLDWMPYFK ALAYGGNFHT VGAVMKPFEV PAFTLIAGDR SISGSATGSP HELRSLMKLA
     GRAKVQPQIE LYPMSKINEA IQHVRDGKAR YRVVLKSDF
//
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