DLD1_YEAST
ID DLD1_YEAST Reviewed; 587 AA.
AC P32891; D6VRH8; Q12360;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=D-lactate dehydrogenase [cytochrome] 1, mitochondrial {ECO:0000303|PubMed:8492799};
DE EC=1.1.2.4 {ECO:0000269|PubMed:8492799};
DE AltName: Full=D-lactate ferricytochrome C oxidoreductase {ECO:0000303|PubMed:8492799};
DE Short=D-LCR {ECO:0000303|PubMed:8492799};
DE Flags: Precursor;
GN Name=DLD1 {ECO:0000303|PubMed:8492799}; Synonyms=DLD;
GN OrderedLocusNames=YDL174C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 204508 / S288c;
RX 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 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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 GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 576-581, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 201238 / W303-1B;
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA 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. {ECO:0000269|PubMed:8492799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome
CC c] + 2 H(+) + pyruvate; Xref=Rhea:RHEA:13521, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.4;
CC Evidence={ECO:0000269|PubMed:8492799};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 2 FAD. {ECO:0000250|UniProtKB:Q5BEJ5};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11502169}.
CC -!- INDUCTION: By D-lactate. Induced during respiratory adaptation.
CC -!- MISCELLANEOUS: Present with 10800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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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 EMBL; BK006938; DAA11688.1; -; Genomic_DNA.
DR PIR; S61038; S61038.
DR RefSeq; NP_010107.1; NM_001180234.1.
DR AlphaFoldDB; P32891; -.
DR SMR; P32891; -.
DR BioGRID; 31892; 79.
DR IntAct; P32891; 15.
DR STRING; 4932.YDL174C; -.
DR UCD-2DPAGE; P32891; -.
DR MaxQB; P32891; -.
DR PaxDb; P32891; -.
DR PRIDE; P32891; -.
DR EnsemblFungi; YDL174C_mRNA; YDL174C; YDL174C.
DR GeneID; 851380; -.
DR KEGG; sce:YDL174C; -.
DR SGD; S000002333; DLD1.
DR VEuPathDB; FungiDB:YDL174C; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_017779_3_3_1; -.
DR InParanoid; P32891; -.
DR OMA; RACNAYS; -.
DR BioCyc; MetaCyc:YDL174C-MON; -.
DR BioCyc; YEAST:YDL174C-MON; -.
DR PRO; PR:P32891; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32891; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IMP:SGD.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:1903457; P:lactate catabolic process; IMP:SGD.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
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 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..587
FT /note="D-lactate dehydrogenase [cytochrome] 1,
FT mitochondrial"
FT /id="PRO_0000020428"
FT DOMAIN 146..327
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CONFLICT 439
FT /note="A -> RR (in Ref. 1; CAA46852)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..587
FT /note="DKIFKTDPNEPANDYR -> GQNL (in Ref. 1; CAA46852)"
FT /evidence="ECO:0000305"
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
