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Database: UniProt
Entry: V5GGD0_BYSSN
LinkDB: V5GGD0_BYSSN
Original site: V5GGD0_BYSSN 
ID   V5GGD0_BYSSN            Unreviewed;       366 AA.
AC   V5GGD0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Alcohol dehydrogenase, putative {ECO:0000313|EMBL:GAD99997.1};
GN   ORFNames=PVAR5_8728 {ECO:0000313|EMBL:GAD99997.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD99997.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={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:GAD99997.1}.
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DR   EMBL; BAUL01000345; GAD99997.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5GGD0; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   InParanoid; V5GGD0; -.
DR   OrthoDB; 820313at2759; -.
DR   Proteomes; UP000018001; 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; 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:SF18; NADP-DEPENDENT ALCOHOL DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_6G00510); 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:UP000018001};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          12..351
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   366 AA;  39680 MW;  BE118B8171AB5502 CRC64;
     MAKSVEFNIF RGSASGEIIP DTSRCALGPF DVFVEVTHAG LCGTDRHFRN KDIALGHEGA
     GVVRQVGSSV TSVQTGDKVG FGWVRKICGH CDYCVSGRDQ YCDEREQYGT HSSEIGSFAS
     HAVWHESMLI KLPDGLEPDY AAPLMCGGAT VWGALTSYNL KPGDRVAIHG IGGLGHMAIQ
     FASALGCDVV VLSSTASKKD EAMQLGAKEF HVTKGDIPEY PIKKVNHLFW CGSANPDYSK
     SVTVFERQFQ VSPSANHSMC RIVALVANDG SIYPLTISYE PPSIPILPIV ANGIKIQGSA
     VASRLAIRKL LRFVVLHGMR PIIMKFPLNK GGIEAAFKTL EEGRMRYRGV LVSQQNLTGK
     PIVEKR
//
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