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Database: UniProt
Entry: C5M6F4_CANTT
LinkDB: C5M6F4_CANTT
Original site: C5M6F4_CANTT 
ID   C5M6F4_CANTT            Unreviewed;       361 AA.
AC   C5M6F4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Enoyl reductase (ER) domain-containing protein {ECO:0000259|SMART:SM00829};
GN   ORFNames=CTRG_01435 {ECO:0000313|EMBL:EER34574.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34574.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER34574.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
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   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
CC   -!- SIMILARITY: Belongs to the YIM1 family.
CC       {ECO:0000256|ARBA:ARBA00038249}.
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DR   EMBL; GG692396; EER34574.1; -; Genomic_DNA.
DR   RefSeq; XP_002547129.1; XM_002547083.1.
DR   AlphaFoldDB; C5M6F4; -.
DR   STRING; 294747.C5M6F4; -.
DR   EnsemblFungi; CTRG_01435-t43_1; CTRG_01435-t43_1-p1; CTRG_01435.
DR   GeneID; 8301323; -.
DR   KEGG; ctp:CTRG_01435; -.
DR   VEuPathDB; FungiDB:CTRG_01435; -.
DR   eggNOG; KOG1198; Eukaryota.
DR   HOGENOM; CLU_026673_3_3_1; -.
DR   OrthoDB; 2013443at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR11695; ALCOHOL DEHYDROGENASE RELATED; 1.
DR   PANTHER; PTHR11695:SF294; RETICULON-4-INTERACTING PROTEIN 1, MITOCHONDRIAL; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037}.
FT   DOMAIN          25..356
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   361 AA;  39275 MW;  DDB6E804DF0934B6 CRC64;
     MTFTSSDLTF NAYSYKNNST PVTLGPETIE LVADSSNPGT FTAPPGKILL KINYTSLNPV
     DVKLHTLAIS LVSMLVNNKN GFGRDFSGQV VAIGENTKTD FKVGDLVQGI YPKVYGKGTA
     SEYLLIDPNE MDITTVPKNI SMIEASSWPT VLGTALLISS DLDYKNKKVL ILGGGTSVGR
     YLVQIAKQRG AKEVAVTCST RTGETLSTIG ADTIIDYTKS KNIVIPILES VKSTGNFDYI
     LDCYGGNDLF TEISNILIKD GRYYTIAGDY PGSSFSCLVS SVSRVVGRSL LRAFGLLSFS
     YKFVMFERFA NNINEARDYL ETGKLKVFID SVYPFDKLDD AVDKLESGRT AGKVVVEVSK
     N
//
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