ID A1D0S8_NEOFI Unreviewed; 378 AA.
AC A1D0S8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EAW24598.1};
GN ORFNames=NFIA_041760 {ECO:0000313|EMBL:EAW24598.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW24598.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027686; EAW24598.1; -; Genomic_DNA.
DR RefSeq; XP_001266495.1; XM_001266494.1.
DR AlphaFoldDB; A1D0S8; -.
DR STRING; 331117.A1D0S8; -.
DR EnsemblFungi; EAW24598; EAW24598; NFIA_041760.
DR GeneID; 4592390; -.
DR KEGG; nfi:NFIA_041760; -.
DR VEuPathDB; FungiDB:NFIA_041760; -.
DR eggNOG; KOG0022; Eukaryota.
DR HOGENOM; CLU_026673_14_1_1; -.
DR OMA; CHTDLSC; -.
DR OrthoDB; 2619844at2759; -.
DR Proteomes; UP000006702; 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:SF11; ENOYL REDUCTASE (ER) DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 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:UP000006702};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..369
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 378 AA; 40231 MW; A5AEFE403B9B05A6 CRC64;
MAYPTEALVV SAVGNEPQFG PVILDTIRDD ELLVEIHATG ICHTDIACIE GKLPAEFPCV
LGHEGAGVVL RPGKGVKDVN VGDKVILSYN FCKDCHQCLS GQPAYCVNLI AQNFGGKRLD
ESRTIRLPNG ETEVFANFFG QSSFCRVALV NRASVARVAA DTPLDIFAPL GCGVQTGAGA
VLNTLNVREG TSVAVFGVGA VGLSAIMAAR LRGASIIIAV DLENSRLEMA RELGATHTLL
GGSEKVLQQI REICAPSNGV EFAVDCSGAT QVIEIMLDSL ATRGRAASVG APAPGKRAGV
DVFSHLTLGR EYVGCHQGSS VAEKMIPYLI EQNKQGKFPV QKLITYYPVE HYQQAFHDLK
VGRAIKAVLL WKESVSNN
//
