ID A6ZXF7_YEAS7 Unreviewed; 587 AA. AC A6ZXF7; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 02-NOV-2016, entry version 45. DE SubName: Full=D-lactate ferricytochrome c oxidoreductase {ECO:0000313|EMBL:EDN60187.1}; GN Name=DLD1 {ECO:0000313|EMBL:EDN60187.1}; GN ORFNames=SCY_0745 {ECO:0000313|EMBL:EDN60187.1}; OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=307796 {ECO:0000313|EMBL:EDN60187.1, ECO:0000313|Proteomes:UP000007060}; RN [1] {ECO:0000313|EMBL:EDN60187.1, ECO:0000313|Proteomes:UP000007060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJM789 {ECO:0000313|EMBL:EDN60187.1, RC ECO:0000313|Proteomes:UP000007060}; RX PubMed=17652520; DOI=10.1073/pnas.0701291104; RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z., RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., RA Wang X., Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., RA Li Y., Davis R.W., Steinmetz L.M.; RT "Genome sequencing and comparative analysis of Saccharomyces RT cerevisiae strain YJM789."; RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EDN60187.1}. 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; AAFW02000145; EDN60187.1; -; Genomic_DNA. DR ProteinModelPortal; A6ZXF7; -. DR SMR; A6ZXF7; -. DR EnsemblFungi; EDN60187; EDN60187; SCY_0745. DR OrthoDB; EOG092C1K74; -. DR Proteomes; UP000007060; Unassembled WGS sequence. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro. DR Gene3D; 1.10.45.10; -; 1. DR Gene3D; 3.30.43.10; -; 1. DR Gene3D; 3.30.465.10; -; 1. DR InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2. DR InterPro; IPR016166; FAD-bd_2. DR InterPro; IPR016167; FAD-bd_2_sub1. DR InterPro; IPR016164; FAD-linked_Oxase-like_C. DR InterPro; IPR004113; FAD-linked_oxidase_C. DR InterPro; IPR006094; Oxid_FAD_bind_N. DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2. DR Pfam; PF02913; FAD-oxidase_C; 1. DR Pfam; PF01565; FAD_binding_4; 1. DR SUPFAM; SSF55103; SSF55103; 1. DR SUPFAM; SSF56176; SSF56176; 1. DR PROSITE; PS51387; FAD_PCMH; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007060}. FT DOMAIN 146 327 FAD-binding PCMH-type. FT {ECO:0000259|PROSITE:PS51387}. SQ SEQUENCE 587 AA; 65293 MW; 07183BEAEEB2EB19 CRC64; MLWKRTCTRL IKPIAQPRGR LVRRSCYRYA STGTGSTDSS SQWLKYSVIA SSATLFGYLF AKNLYSRETK EDLIEKLEMV KKIDPVNSTL KLSSLDSPDY LHDPVKIDKV VEDLKQVLGN KPENYSDAKS DLDAHSDTYF NTHHPSPEQR PRIILFPHTT EEVSKILKIC HDNNMPVVPF SGGTSLEGHF LPTRIGDTIT VDLSKFMNNV VKFDKLDLDI TVQAGLPWED LNDYLSDHGL MFGCDPGPGA QIGGCIANSC SGTNAYRYGT MKENIINMTI VLPDGTIVKT KKRPRKSSAG YNLNGLFVGS EGTLGIVTEA TVKCHVKPKA ETVAVVSFDT IKDAAACASN LTQSGIHLNA MELLDENMMK LINASESTDR CDWVEKPTMF FKIGGRSPNI VNALVDEVKA VAQLNHCNSF QFAKDDDEKL ELWEARKVAL WSVLDADKSK DKSAKIWTTD VAVPVSQFDK VIHETKKDMQ ASKLINAIVG HAGDGNFHAF IVYRTPEEHE TCSQLVDRMV KRALNAEGTC TGEHGVGIGK REYLLEELGE APVDLMRKIK LAIDPKRIMN PDKIFKTDPN EPANDYR //