ID   DLD1_YEAST              Reviewed;         587 AA.
AC   P32891; Q12360;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-NOV-2008, entry version 79.
DE   RecName: Full=D-lactate dehydrogenase [cytochrome] 1, mitochondrial;
DE            EC=1.1.2.4;
DE   AltName: Full=D-lactate ferricytochrome C oxidoreductase;
DE            Short=D-LCR;
DE   Flags: Precursor;
GN   Name=DLD1; Synonyms=DLD; OrderedLocusNames=YDL174C;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=93261413; PubMed=8492799; DOI=10.1007/BF00291989;
RA   Lodi T., Ferrero I.;
RT   "Isolation of the DLD gene of Saccharomyces cerevisiae encoding the
RT   mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase.";
RL   Mol. Gen. Genet. 238:315-324(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 576-581, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 201238 / W303-1B;
RX   MEDLINE=21393706; PubMed=11502169; DOI=10.1021/bi010277r;
RA   Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N.,
RA   Manon S., Schmitter J.-M.;
RT   "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT   complex.";
RL   Biochemistry 40:9758-9769(2001).
RN   [4]
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).
CC   -!- FUNCTION: Catalyzes the stereospecific oxidation of D-lactate to
CC       pyruvate.
CC   -!- CATALYTIC ACTIVITY: (R)-lactate + 2 ferricytochrome c = pyruvate +
CC       2 ferrocytochrome c.
CC   -!- COFACTOR: Binds 2 FAD.
CC   -!- COFACTOR: Binds 4-6 zinc ions.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- INDUCTION: By D-lactate. Induced during respiratory adaptation.
CC   -!- MISCELLANEOUS: Present with 10800 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; X66052; CAA46852.1; -; Genomic_DNA.
DR   EMBL; Z67750; CAA91571.1; -; Genomic_DNA.
DR   EMBL; Z74222; CAA98748.1; -; Genomic_DNA.
DR   PIR; S61038; S61038.
DR   RefSeq; NP_010107.1; -.
DR   PeptideAtlas; P32891; -.
DR   Ensembl; YDL174C; Saccharomyces cerevisiae.
DR   GeneID; 851380; -.
DR   GenomeReviews; Z71256_GR; YDL174C.
DR   KEGG; sce:YDL174C; -.
DR   NMPDR; fig|4932.3.peg.841; -.
DR   CYGD; YDL174c; -.
DR   SGD; S000002333; DLD1.
DR   HOGENOM; P32891; -.
DR   LinkHub; P32891; -.
DR   NextBio; 968519; -.
DR   ArrayExpress; P32891; -.
DR   GermOnline; YDL174C; Saccharomyces cerevisiae.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:EC.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IMP:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
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   Gene3D; G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 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; Direct protein sequencing; FAD; Flavoprotein;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Transit peptide; Zinc.
FT   TRANSIT       1      ?       Mitochondrion.
FT   CHAIN         ?    587       D-lactate dehydrogenase [cytochrome] 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000020428.
FT   DOMAIN      146    327       FAD-binding PCMH-type.
FT   CONFLICT    439    439       A -> RR (in Ref. 1; CAA46852).
FT   CONFLICT    572    587       DKIFKTDPNEPANDYR -> GQNL (in Ref. 1;
FT                                CAA46852).
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
//