ID   DLD1_KLULA              Reviewed;         576 AA.
AC   Q12627; Q6CMJ7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   25-NOV-2008, entry version 61.
DE   RecName: Full=D-lactate dehydrogenase [cytochrome], 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=KLLA0E19789g;
OS   Kluyveromyces lactis (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=28985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
RX   MEDLINE=95058916; PubMed=7969031; DOI=10.1007/BF00282752;
RA   Lodi T., O'Connor D., Goffrini P., Ferrero I.;
RT   "Carbon catabolite repression in Kluyveromyces lactis: isolation and
RT   characterization of the KIDLD gene encoding the mitochondrial enzyme
RT   D-lactate ferricytochrome c oxidoreductase.";
RL   Mol. Gen. Genet. 244:622-629(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 matrix.
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; X71628; CAA50635.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99929.1; -; Genomic_DNA.
DR   PIR; S51528; S51528.
DR   RefSeq; XP_454842.1; -.
DR   GeneID; 2894285; -.
DR   KEGG; kla:KLLA0E19789g; -.
DR   HOGENOM; Q12627; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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: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   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW   Transit peptide; Zinc.
FT   TRANSIT       1      ?       Mitochondrion.
FT   CHAIN         ?    576       D-lactate dehydrogenase [cytochrome],
FT                                mitochondrial.
FT                                /FTId=PRO_0000020427.
FT   DOMAIN      139    320       FAD-binding PCMH-type.
FT   CONFLICT    539    539       E -> Q (in Ref. 1; CAA50635).
FT   CONFLICT    564    564       D -> DKIF (in Ref. 1; CAA50635).
SQ   SEQUENCE   576 AA;  63097 MW;  629615C88758545F CRC64;
     MFRFVGRSGF ALRGSLQLRK DVLRSRTTAV AKRHYSSSNG NNGGGFSSAI LSVLGGSLIG
     GGFVAYALGS QFEKEKSVSD LSIARLEDLD SPEYCDKETF AKALVELKDV LENDPENFTV
     AKDDLDAHSD TYFNSHHAEA NQRPEIVLYP RNTEDVSKLL KICHKYSIPV IPFSGGTSLE
     GHFLPTRPGS CVVLDISKYL NKIIQLNKED LDVVVQGGVP WEELNEYLND HGLLFGCDPG
     PGAQIAGCIA NSCSGTNAYR YGTMKENVVN ITMCMADGTI VKTKRRPRKS SAGYNLNGLI
     IGSEGTLGIV TEATIKCHVR STFETVAVVP FPTVSDAASC SSHLIQAGIQ LNAMELLDDN
     MMKIINQSGA TSKDNWVESP TLFFKIGGRS EQIIQEVIKE VEKIASQHNN TKFEFATDED
     SKLELWEARK VALWSTIDTG RKTNPDANIW TTDVAVPISK FADVINATKE EMNASGLLTS
     LVGHAGDGNF HAFIIYNTEQ RKTAETIVEN MVKRAIDAEG TCTGEHGVGI GKRDYLLEEV
     GEDTVAVMRK LKLALDPKRI LNPDKIFKID PNDHQH
//