ID A1CVA6_NEOFI Unreviewed; 361 AA.
AC A1CVA6;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013190};
DE EC=1.1.1.1 {ECO:0000256|ARBA:ARBA00013190};
GN ORFNames=NFIA_045020 {ECO:0000313|EMBL:EAW25683.1};
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:EAW25683.1, 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|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR EMBL; DS027684; EAW25683.1; -; Genomic_DNA.
DR RefSeq; XP_001267580.1; XM_001267579.1.
DR AlphaFoldDB; A1CVA6; -.
DR STRING; 331117.A1CVA6; -.
DR EnsemblFungi; EAW25683; EAW25683; NFIA_045020.
DR GeneID; 4594242; -.
DR KEGG; nfi:NFIA_045020; -.
DR VEuPathDB; FungiDB:NFIA_045020; -.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_1_1; -.
DR OMA; CWDDKET; -.
DR OrthoDB; 5295198at2759; -.
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; cd08297; CAD3; 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; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR PANTHER; PTHR42940:SF1; ENOYL REDUCTASE (ER) DOMAIN-CONTAINING PROTEIN; 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 21..357
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 361 AA; 38241 MW; 1CE597C46113B013 CRC64;
MDSKIYDIPT HCKAGVVVNE GPDFQVKVEM VPVPEPGPDD ILIRLNVTGL CSSDIHMMKN
DLGTPPMSFF GVRSPGHEGA GIVVKTGANV RNFKVGDRAG IKPLTDTCGS CELCWDDKET
YCRTAVHTGL MTAGTYQQYI VSPARYASPI PDGVPDEIAA PIMCSASTIY RSLVESGLRP
GHWAVFPGGG GGVGIQGVQL ARAMGMRPIV VDTGPAKRAL ALEMGAEAFV DFAETEDTTA
AVVAAADGIG AHGVFVTAPA AYRTALSFVG DRVGAVVMCI GLAPAKTMVV GDDPNRFIFK
NLTIKGTLVG SRKDTAAALD FARRGMLKQI CEVYPIDRLP EAVEKLRRGE VAGRIVVDFD
Q
//
