ID B2KJ46_CANPA Unreviewed; 279 AA. AC B2KJ46; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 29-MAY-2024, entry version 76. DE SubName: Full=Carbonyl Reductase {ECO:0000313|PDB:3CTM}; DE EC=1.1.1.- {ECO:0000313|PDB:3CTM}; DE SubName: Full=S-reductase {ECO:0000313|EMBL:ABG57118.1}; DE SubName: Full=Sorbose reductase SOU1 {ECO:0000313|EMBL:KAF6048739.1}; DE Flags: Fragment; GN Name=SOU1 {ECO:0000313|EMBL:KAF6048739.1}; GN ORFNames=DQ675534 {ECO:0000313|PDB:3CTM}, FOB60_004123 GN {ECO:0000313|EMBL:KAF6048739.1}; OS Candida parapsilosis (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=5480 {ECO:0000313|EMBL:ABG57118.1}; RN [1] {ECO:0000313|EMBL:ABG57118.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCTCCM 20311 {ECO:0000313|EMBL:ABG57118.1}; RX PubMed=17435004; DOI=10.1128/AEM.02185-06; RA Nie Y., Xu Y., Mu X.Q., Wang H.Y., Yang M., Xiao R.; RT "Purification, characterization, gene cloning, and expression of a novel RT alcohol dehydrogenase with anti-prelog stereospecificity from Candida RT parapsilosis."; RL Appl. Environ. Microbiol. 73:3759-3764(2007). RN [2] {ECO:0000313|PDB:3CTM, ECO:0007829|PDB:3CTM} RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS). RX PubMed=18566346; DOI=10.1110/ps.035089.108; RA Zhang R., Zhu G., Zhang W., Cao S., Ou X., Li X., Bartlam M., Xu Y., RA Zhang X.C., Rao Z.; RT "Crystal structure of a carbonyl reductase from Candida parapsilosis with RT anti-Prelog stereospecificity."; RL Protein Sci. 17:1412-1423(2008). RN [3] {ECO:0000313|EMBL:KAF6048739.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_652 {ECO:0000313|EMBL:KAF6048739.1}; RA Campos J., Goldberg B., Tallon L., Sadzewicz L., Vavikolanu K., Mehta A., RA Aluvathingal J., Nadendla S., Nandy P., Geyer C., Yan Y., Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000256|ARBA:ARBA00006484}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ675534; ABG57118.1; -; Genomic_DNA. DR EMBL; JABWAB010000006; KAF6048739.1; -; Genomic_DNA. DR PDB; 3CTM; X-ray; 2.69 A; A/B/C/D/E/F/G/H=1-279. DR PDBsum; 3CTM; -. DR AlphaFoldDB; B2KJ46; -. DR SMR; B2KJ46; -. DR EnsemblFungi; CPAR2_501160-T; CPAR2_501160-T-p1; CPAR2_501160. DR VEuPathDB; FungiDB:CPAR2_501160; -. DR OrthoDB; 662155at2759; -. DR BRENDA; 1.1.1.1; 1133. DR BRENDA; 1.1.1.184; 1133. DR EvolutionaryTrace; B2KJ46; -. DR Proteomes; UP000590412; Unassembled WGS sequence. DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IEA:TreeGrafter. DR GO; GO:0008152; P:metabolic process; IEA:UniProt. DR CDD; cd05352; MDH-like_SDR_c; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR002347; SDR_fam. DR PANTHER; PTHR43008; BENZIL REDUCTASE; 1. DR PANTHER; PTHR43008:SF13; L-XYLULOSE REDUCTASE-RELATED; 1. DR Pfam; PF13561; adh_short_C2; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000313|PDB:3CTM, ECO:0007829|PDB:3CTM}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT NON_TER 279 FT /evidence="ECO:0000313|EMBL:ABG57118.1" SQ SEQUENCE 279 AA; 30089 MW; A7E94F2DF6E4A6B0 CRC64; MGEIESYCNK ELGPLPTKAP TLSKNVLDLF SLKGKVASVT GSSGGIGWAV AEAYAQAGAD VAIWYNSHPA DEKAEHLQKT YGVHSKAYKC NISDPKSVEE TISQQEKDFG TIDVFVANAG VTWTQGPEID VDNYDSWNKI ISVDLNGVYY CSHNIGKIFK KNGKGSLIIT SSISGKIVNI PQLQAPYNTA KAACTHLAKS LAIEWAPFAR VNTISPGYID TDITDFASKD MKAKWWQLTP LGREGLTQEL VGGYLYLASN ASTFTTGSDV VIDGGYTCP //