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Protein

D-lactate dehydrogenase [cytochrome] 1, mitochondrial

Gene

DLD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the stereospecific oxidation of D-lactate to pyruvate.

Catalytic activityi

(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H+.

Cofactori

Protein has several cofactor binding sites:
  • FADNote: Binds 2 FAD.
  • Zn2+Note: Binds 4 to 6 Zn2+ ions.

GO - Molecular functioni

  • D-lactate dehydrogenase (cytochrome) activity Source: SGD
  • flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  • lactate catabolic process Source: SGD
  • protein targeting to mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, Zinc

Enzyme and pathway databases

BioCyciYEAST:YDL174C-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
D-lactate dehydrogenase [cytochrome] 1, mitochondrial (EC:1.1.2.4)
Alternative name(s):
D-lactate ferricytochrome C oxidoreductase
Short name:
D-LCR
Gene namesi
Name:DLD1
Synonyms:DLD
Ordered Locus Names:YDL174C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL174C.
SGDiS000002333. DLD1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: SGD
  • mitochondrial intermembrane space Source: Reactome
  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 587D-lactate dehydrogenase [cytochrome] 1, mitochondrialPRO_0000020428
Transit peptidei1 – ?Mitochondrion

Proteomic databases

MaxQBiP32891.

2D gel databases

UCD-2DPAGEP32891.

Expressioni

Inductioni

By D-lactate. Induced during respiratory adaptation.

Interactioni

Protein-protein interaction databases

BioGridi31892. 22 interactions.
IntActiP32891. 15 interactions.
MINTiMINT-4479737.

Structurei

3D structure databases

ProteinModelPortaliP32891.
SMRiP32891. Positions 148-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini146 – 327182FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063515.
HOGENOMiHOG000230995.
InParanoidiP32891.
KOiK00102.
OMAiGAFEIRV.
OrthoDBiEOG7DC2DX.

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32891-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLWKRTCTRL IKPIAQPRGR LVRRSCYRYA STGTGSTDSS SQWLKYSVIA
60 70 80 90 100
SSATLFGYLF AKNLYSRETK EDLIEKLEMV KKIDPVNSTL KLSSLDSPDY
110 120 130 140 150
LHDPVKIDKV VEDLKQVLGN KPENYSDAKS DLDAHSDTYF NTHHPSPEQR
160 170 180 190 200
PRIILFPHTT EEVSKILKIC HDNNMPVVPF SGGTSLEGHF LPTRIGDTIT
210 220 230 240 250
VDLSKFMNNV VKFDKLDLDI TVQAGLPWED LNDYLSDHGL MFGCDPGPGA
260 270 280 290 300
QIGGCIANSC SGTNAYRYGT MKENIINMTI VLPDGTIVKT KKRPRKSSAG
310 320 330 340 350
YNLNGLFVGS EGTLGIVTEA TVKCHVKPKA ETVAVVSFDT IKDAAACASN
360 370 380 390 400
LTQSGIHLNA MELLDENMMK LINASESTDR CDWVEKPTMF FKIGGRSPNI
410 420 430 440 450
VNALVDEVKA VAQLNHCNSF QFAKDDDEKL ELWEARKVAL WSVLDADKSK
460 470 480 490 500
DKSAKIWTTD VAVPVSQFDK VIHETKKDMQ ASKLINAIVG HAGDGNFHAF
510 520 530 540 550
IVYRTPEEHE TCSQLVDRMV KRALNAEGTC TGEHGVGIGK REYLLEELGE
560 570 580
APVDLMRKIK LAIDPKRIMN PDKIFKTDPN EPANDYR
Length:587
Mass (Da):65,293
Last modified:November 1, 1997 - v2
Checksum:i07183BEAEEB2EB19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391A → RR in CAA46852 (PubMed:8492799).Curated
Sequence conflicti572 – 58716DKIFK…ANDYR → GQNL in CAA46852 (PubMed:8492799).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66052 Genomic DNA. Translation: CAA46852.1.
Z67750 Genomic DNA. Translation: CAA91571.1.
Z74222 Genomic DNA. Translation: CAA98748.1.
BK006938 Genomic DNA. Translation: DAA11688.1.
PIRiS61038.
RefSeqiNP_010107.1. NM_001180234.1.

Genome annotation databases

EnsemblFungiiYDL174C; YDL174C; YDL174C.
GeneIDi851380.
KEGGisce:YDL174C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66052 Genomic DNA. Translation: CAA46852.1.
Z67750 Genomic DNA. Translation: CAA91571.1.
Z74222 Genomic DNA. Translation: CAA98748.1.
BK006938 Genomic DNA. Translation: DAA11688.1.
PIRiS61038.
RefSeqiNP_010107.1. NM_001180234.1.

3D structure databases

ProteinModelPortaliP32891.
SMRiP32891. Positions 148-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31892. 22 interactions.
IntActiP32891. 15 interactions.
MINTiMINT-4479737.

2D gel databases

UCD-2DPAGEP32891.

Proteomic databases

MaxQBiP32891.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL174C; YDL174C; YDL174C.
GeneIDi851380.
KEGGisce:YDL174C.

Organism-specific databases

EuPathDBiFungiDB:YDL174C.
SGDiS000002333. DLD1.

Phylogenomic databases

GeneTreeiENSGT00530000063515.
HOGENOMiHOG000230995.
InParanoidiP32891.
KOiK00102.
OMAiGAFEIRV.
OrthoDBiEOG7DC2DX.

Enzyme and pathway databases

BioCyciYEAST:YDL174C-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Miscellaneous databases

PROiP32891.

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase."
    Lodi T., Ferrero I.
    Mol. Gen. Genet. 238:315-324(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    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.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 576-581, SUBCELLULAR LOCATION.
    Strain: ATCC 201238 / W303-1B.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDLD1_YEAST
AccessioniPrimary (citable) accession number: P32891
Secondary accession number(s): D6VRH8, Q12360
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.