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D-lactate dehydrogenase [cytochrome] 1, mitochondrial (EC 1.1.2.4) (D-lactate ferricytochrome C oxidoreductase) (D-LCR)

 DLD1_YEAST              Reviewed;         587 AA.
P32891; D6VRH8; Q12360;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 158.
RecName: Full=D-lactate dehydrogenase [cytochrome] 1, mitochondrial;
EC=1.1.2.4;
AltName: Full=D-lactate ferricytochrome C oxidoreductase;
Short=D-LCR;
Flags: Precursor;
Name=DLD1; Synonyms=DLD; OrderedLocusNames=YDL174C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8492799; DOI=10.1007/BF00291989;
Lodi T., Ferrero I.;
"Isolation of the DLD gene of Saccharomyces cerevisiae encoding the
mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase.";
Mol. Gen. Genet. 238:315-324(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEIN SEQUENCE OF 576-581, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 201238 / W303-1B;
PubMed=11502169; DOI=10.1021/bi010277r;
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N.,
Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular
complex.";
Biochemistry 40:9758-9769(2001).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
-!- FUNCTION: Catalyzes the stereospecific oxidation of D-lactate to
pyruvate.
-!- CATALYTIC ACTIVITY: (R)-lactate + 2 ferricytochrome c = pyruvate +
2 ferrocytochrome c + 2 H(+).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 2 FAD.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 4 to 6 Zn(2+) ions.;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:11502169}.
-!- INDUCTION: By D-lactate. Induced during respiratory adaptation.
-!- MISCELLANEOUS: Present with 10800 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase
type 4 family. {ECO:0000305}.
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EMBL; X66052; CAA46852.1; -; Genomic_DNA.
EMBL; Z67750; CAA91571.1; -; Genomic_DNA.
EMBL; Z74222; CAA98748.1; -; Genomic_DNA.
EMBL; BK006938; DAA11688.1; -; Genomic_DNA.
PIR; S61038; S61038.
RefSeq; NP_010107.1; NM_001180234.1.
ProteinModelPortal; P32891; -.
SMR; P32891; -.
BioGrid; 31892; 72.
IntAct; P32891; 15.
MINT; MINT-4479737; -.
STRING; 4932.YDL174C; -.
UCD-2DPAGE; P32891; -.
MaxQB; P32891; -.
PRIDE; P32891; -.
EnsemblFungi; YDL174C; YDL174C; YDL174C.
GeneID; 851380; -.
KEGG; sce:YDL174C; -.
EuPathDB; FungiDB:YDL174C; -.
SGD; S000002333; DLD1.
GeneTree; ENSGT00530000063515; -.
HOGENOM; HOG000230995; -.
InParanoid; P32891; -.
KO; K00102; -.
OMA; TPRTCGE; -.
OrthoDB; EOG092C1K74; -.
BioCyc; YEAST:YDL174C-MONOMER; -.
PRO; PR:P32891; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IMP:SGD.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:1903457; P:lactate catabolic process; IMP:SGD.
GO; GO:0006626; P:protein targeting to mitochondrion; TAS:Reactome.
Gene3D; 1.10.45.10; -; 1.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR016164; FAD-linked_Oxase-like_C.
InterPro; IPR004113; FAD-linked_oxidase_C.
InterPro; IPR006094; Oxid_FAD_bind_N.
InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
Pfam; PF02913; FAD-oxidase_C; 1.
Pfam; PF01565; FAD_binding_4; 1.
SUPFAM; SSF55103; SSF55103; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS51387; FAD_PCMH; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; FAD; Flavoprotein;
Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
Reference proteome; Transit peptide; Zinc.
TRANSIT 1 ? Mitochondrion.
CHAIN ? 587 D-lactate dehydrogenase [cytochrome] 1,
mitochondrial.
/FTId=PRO_0000020428.
DOMAIN 146 327 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
CONFLICT 439 439 A -> RR (in Ref. 1; CAA46852).
{ECO:0000305}.
CONFLICT 572 587 DKIFKTDPNEPANDYR -> GQNL (in Ref. 1;
CAA46852). {ECO:0000305}.
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


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