ID F0XC25_GROCL Unreviewed; 387 AA.
AC F0XC25;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EFX04122.1};
GN ORFNames=CMQ_1050 {ECO:0000313|EMBL:EFX04122.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX04122.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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}.
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DR EMBL; GL629765; EFX04122.1; -; Genomic_DNA.
DR RefSeq; XP_014173604.1; XM_014318129.1.
DR AlphaFoldDB; F0XC25; -.
DR STRING; 655863.F0XC25; -.
DR GeneID; 25973886; -.
DR eggNOG; KOG0022; Eukaryota.
DR HOGENOM; CLU_026673_14_1_1; -.
DR InParanoid; F0XC25; -.
DR OrthoDB; 2619844at2759; -.
DR Proteomes; UP000007796; 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; cd08278; benzyl_alcohol_DH; 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; 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:UP000007796};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 12..385
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 387 AA; 40613 MW; A075841049CDA8C9 CRC64;
MAFETEALVA RGPFSEGKWA IEPVVLRALG PDEVLVEMVA SGICHTDLHC GNTAADAGVP
SVFYPRVLGH EGSGYVVQAG RAVTKVKPGD AVLLSFSYCG ECYVCQAGTP SHCLRFFDIN
FLGEPVFAPR TADSSSAAVT ATIGGRFFGQ SSFARHAIVS AQSVVNVSSL QLSRADLRLL
APLGCGFQTG SATVINVAQA GPDDSVTIVG MGGVGLAAVI AAHNRGCRAV IGVDRVEARL
ALARSLGATH TVNTTGRSMD EVAALIRAAT VDGLGSSISI DTSAHPPLLA AQIDAARYMG
RIIQVGTGMP DAHVELHMQS FMVSGKQYFG AVQGRVQPEA YVPTMVQWWR DGIFPVEKLV
TFFEATDFAS AIKAMGSSDV IKPVIVW
//
