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Database: UniProt
Entry: C4YEG3_CANAW
LinkDB: C4YEG3_CANAW
Original site: C4YEG3_CANAW 
ID   C4YEG3_CANAW            Unreviewed;       394 AA.
AC   C4YEG3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CAWG_00920 {ECO:0000313|EMBL:EEQ42699.1};
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ42699.1, ECO:0000313|Proteomes:UP000001429};
RN   [1] {ECO:0000313|EMBL:EEQ42699.1, ECO:0000313|Proteomes:UP000001429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1 {ECO:0000313|EMBL:EEQ42699.1,
RC   ECO:0000313|Proteomes:UP000001429};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH672346; EEQ42699.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YEG3; -.
DR   PaxDb; 5476-C4YEG3; -.
DR   VEuPathDB; FungiDB:CAWG_00920; -.
DR   HOGENOM; CLU_026673_11_0_1; -.
DR   OMA; LFCGHCA; -.
DR   Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08233; butanediol_DH_like; 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   PANTHER; PTHR43161:SF23; (R,R)-BUTANEDIOL DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          27..160
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          203..335
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   394 AA;  43085 MW;  94383610FD50A7B0 CRC64;
     MKAIVYHDRG DIRYDPNFPD PQIIRSDDVK IKVHYCGICG TDLKEYSDGP IFFPPKGELN
     EISQMESIQV MGHEISGEVI AIGDDVTNVK VGDKVVVEVT GTCLDRHRYQ DPKNGDSPKP
     NCPSCVSGNY NACDYLALIG CGFANGGCAE YLVVASSKVI AFDQNKIPMD IAALIQPIAV
     SWHAVKVSNF KPGSNALILG GGPIGLTTIF ALKGNQVSQI VLSEPALARR QLAEKLGVIT
     YDPTGKSIEQ CVEDLKKLSP GGYGYEYSYD CSGVKATFET GLKTLKIRGC ATNVAIWAHK
     SIPLYPMEIT LSEKMLTGSI CFVKKDFEES IKAIENGLIS IDELKMLITS KIHLQDGIEK
     GFLELINHKE KHIKILFSPK SEYLLCNGVN DSNK
//
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