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Database: UniProt
Entry: A1C8K3_ASPCL
LinkDB: A1C8K3_ASPCL
Original site: A1C8K3_ASPCL 
ID   A1C8K3_ASPCL            Unreviewed;       359 AA.
AC   A1C8K3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   SubName: Full=Zinc-binding alcohol dehydrogenase, putative {ECO:0000313|EMBL:EAW13640.1};
GN   ORFNames=ACLA_043600 {ECO:0000313|EMBL:EAW13640.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13640.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW13640.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
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|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; DS027046; EAW13640.1; -; Genomic_DNA.
DR   RefSeq; XP_001275066.1; XM_001275065.1.
DR   AlphaFoldDB; A1C8K3; -.
DR   STRING; 344612.A1C8K3; -.
DR   EnsemblFungi; EAW13640; EAW13640; ACLA_043600.
DR   GeneID; 4707362; -.
DR   KEGG; act:ACLA_043600; -.
DR   VEuPathDB; FungiDB:ACLA_043600; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   OMA; YCDGGYS; -.
DR   OrthoDB; 5353053at2759; -.
DR   Proteomes; UP000006701; 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:SF82; ALCOHOL DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02430)-RELATED; 1.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 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:UP000006701};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          17..355
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   359 AA;  38738 MW;  B0125D613E92E5EA CRC64;
     MSSTDYKFEG WMGLDNQSIG NMVWKDFKPK EWEETDVDIK ITHSGICGSD LHTLRSGWGP
     SRYPCCVGHE IVGIAVRVGS KAEGGIKVGD RVGVGAQNDS CLGRKGDCEE CASGLEQYCV
     NMVGTYNAVH FNGDKSYGGY ALYHRAPSHF VMKIPDAIPS AEAAPMLCGG VTLYSPLKHY
     GCGPGKKVGV IGIGGLGHFG ILFAKAMGAD KVVAISRKAN KKEDALKLGA DEYIATDDDQ
     DWAKKHGRSL DLIVSTVSSS KMPIVQYASL LRTNGAFVQM GAPEDGALEI PAMSLISRRI
     RMGGSLIGSP SELREMLQLA ADKGVHPWIQ ERSMKDANQA VLDMDAGKAR YRYVLVNDQ
//
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