ID   DLD3_YEAST              Reviewed;         496 AA.
AC   P39976;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-NOV-2008, entry version 65.
DE   RecName: Full=D-lactate dehydrogenase [cytochrome] 3;
DE            EC=1.1.2.4;
DE   AltName: Full=D-lactate ferricytochrome C oxidoreductase;
DE            Short=D-LCR;
GN   Name=DLD3; OrderedLocusNames=YEL071W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313264; PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10509019;
RX   DOI=10.1002/(SICI)1097-0061(19990930)15:13<1377::AID-YEA473>3.0.CO;2-0;
RA   Chelstowska A., Liu Z., Jia Y., Amberg D., Butow R.A.;
RT   "Signalling between mitochondria and the nucleus regulates the
RT   expression of a new D-lactate dehydrogenase activity in yeast.";
RL   Yeast 15:1377-1391(1999).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-17, AND MASS
RP   SPECTROMETRY.
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,
RA   Marsischky G., Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- CATALYTIC ACTIVITY: (R)-lactate + 2 ferricytochrome c = pyruvate +
CC       2 ferrocytochrome c.
CC   -!- COFACTOR: FAD (Potential).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 13000 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase
CC       type 4 family.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR   EMBL; U18795; AAB65016.1; -; Genomic_DNA.
DR   PIR; S50518; S50518.
DR   RefSeq; NP_010843.1; -.
DR   DIP; DIP:6418N; -.
DR   PeptideAtlas; P39976; -.
DR   Ensembl; YEL071W; Saccharomyces cerevisiae.
DR   GeneID; 856638; -.
DR   GenomeReviews; U00092_GR; YEL071W.
DR   KEGG; sce:YEL071W; -.
DR   NMPDR; fig|4932.3.peg.1891; -.
DR   CYGD; YEL071w; -.
DR   SGD; S000000797; DLD3.
DR   HOGENOM; P39976; -.
DR   LinkHub; P39976; -.
DR   NextBio; 982595; -.
DR   ArrayExpress; P39976; -.
DR   GermOnline; YEL071W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005625; C:soluble fraction; IDA:SGD.
DR   GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:EC.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Gene3D; G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Oxidoreductase;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    496       D-lactate dehydrogenase [cytochrome] 3.
FT                                /FTId=PRO_0000128176.
FT   DOMAIN       64    243       FAD-binding PCMH-type.
FT   MOD_RES     470    470       Phosphoserine.
FT   CROSSLNK     17     17       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
SQ   SEQUENCE   496 AA;  55225 MW;  4809F74EDF07F520 CRC64;
     MTAAHPVAQL TAEAYPKVKR NPNFKVLDSE DLAYFRSILS NDEILNSQAP EELASFNQDW
     MKKYRGQSNL ILLPNSTDKV SKIMKYCNDK KLAVVPQGGN TDLVGASVPV FDEIVLSLRN
     MNKVRDFDPV SGTFKCDAGV VMRDAHQFLH DHDHIFPLDL PSRNNCQVGG VVSTNAGGLN
     FLRYGSLHGN VLGLEVVLPN GEIISNINAL RKDNTGYDLK QLFIGAEGTI GVVTGVSIVA
     AAKPKALNAV FFGIENFDTV QKLFVKAKSE LSEILSAFEF MDRGSIECTI EYLKDLPFPL
     ENQHNFYVLI ETSGSNKRHD DEKLTAFLKD TTDSKLISEG MMAKDKADFD RLWTWRKSVP
     TACNSYGGMY KYDMSLQLKD LYSVSAAVTE RLNAAGLIGD APKPVVKSCG YGHVGDGNIH
     LNIAVREFTK QIEDLLEPFV YEYIASKKGS ISAEHGIGFH KKGKLHYTRS DIEIRFMKDI
     KNHYDPNGIL NPYKYI
//