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Protein

D-lactate dehydrogenase [cytochrome] 2, mitochondrial

Gene

DLD2

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

In addition to its enzymatic role it could play an important role in the yeast cell morphology.1 Publication

Catalytic activityi

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

Cofactori

FADCurated

GO - Molecular functioni

  • (R)-2-hydroxyglutarate dehydrogenase activity Source: SGD
  • actin binding Source: SGD
  • D-lactate dehydrogenase (cytochrome) activity Source: SGD
  • FAD binding Source: SGD

GO - Biological processi

  • lactate catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciYEAST:YDL178W-MONOMER.
ReactomeiR-SCE-880009. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

Names & Taxonomyi

Protein namesi
Recommended name:
D-lactate dehydrogenase [cytochrome] 2, mitochondrial (EC:1.1.2.4)
Alternative name(s):
Actin-interacting protein 2
D-lactate ferricytochrome C oxidoreductase
Short name:
D-LCR
Gene namesi
Name:DLD2
Synonyms:AIP2
Ordered Locus Names:YDL178W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL178W.
SGDiS000002337. DLD2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 530D-lactate dehydrogenase [cytochrome] 2, mitochondrialPRO_0000020429
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

MaxQBiP46681.
PeptideAtlasiP46681.

Interactioni

Subunit structurei

Interacts with F-actin.1 Publication

GO - Molecular functioni

  • actin binding Source: SGD

Protein-protein interaction databases

BioGridi31888. 16 interactions.
DIPiDIP-956N.
MINTiMINT-4479766.

Structurei

3D structure databases

ProteinModelPortaliP46681.
SMRiP46681. Positions 28-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 277180FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000075086.
HOGENOMiHOG000230997.
InParanoidiP46681.
KOiK00102.
OMAiNEDWMRK.
OrthoDBiEOG7SJDDF.

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.

P46681-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRNILVRST GSNFKFAGRY MKSSALLGYY RRVNYYSTKI QTRLTSENYP
60 70 80 90 100
DVHRDPRFKK LTSDDLNYFK SILSEQEILR ASESEDLSFY NEDWMRKYKG
110 120 130 140 150
QSKLVLRPKS VEKVSLILNY CNDEKIAVVP QGGNTGLVGG SVPIFDELIL
160 170 180 190 200
SLANLNKIRD FDPVSGILKC DAGVILENAN NYVMEQNYMF PLDLGAKGSC
210 220 230 240 250
HVGGVVATNA GGLRLLRYGS LHGSVLGLEV VMPNGQIVNS MHSMRKDNTG
260 270 280 290 300
YDLKQLFIGS EGTIGIITGV SILTVPKPKA FNVSYLSVES FEDVQKVFVR
310 320 330 340 350
ARQELSEILS AFEFMDAKSQ VLAKSQLKDA AFPLEDEHPF YILIETSGSN
360 370 380 390 400
KDHDDSKLET FLENVMEEGI VTDGVVAQDE TELQNLWKWR EMIPEASQAN
410 420 430 440 450
GGVYKYDVSL PLKDLYSLVE ATNARLSEAE LVGDSPKPVV GAIGYGHVGD
460 470 480 490 500
GNLHLNVAVR EYNKNIEKTL EPFVYEFVSS KHGSVSAEHG LGFQKKNYIG
510 520 530
YSKSPEEVKM MKDLKVHYDP NGILNPYKYI
Length:530
Mass (Da):59,268
Last modified:November 1, 1995 - v1
Checksum:i42FDFBE5CA7E11B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391N → S in AAU09682 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35667 Genomic DNA. Translation: AAA79142.1.
Z67750 Genomic DNA. Translation: CAA91567.1.
Z74226 Genomic DNA. Translation: CAA98752.1.
AY723765 Genomic DNA. Translation: AAU09682.1.
BK006938 Genomic DNA. Translation: DAA11684.1.
PIRiS61034.
RefSeqiNP_010103.1. NM_001180238.1.

Genome annotation databases

EnsemblFungiiYDL178W; YDL178W; YDL178W.
GeneIDi851376.
KEGGisce:YDL178W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35667 Genomic DNA. Translation: AAA79142.1.
Z67750 Genomic DNA. Translation: CAA91567.1.
Z74226 Genomic DNA. Translation: CAA98752.1.
AY723765 Genomic DNA. Translation: AAU09682.1.
BK006938 Genomic DNA. Translation: DAA11684.1.
PIRiS61034.
RefSeqiNP_010103.1. NM_001180238.1.

3D structure databases

ProteinModelPortaliP46681.
SMRiP46681. Positions 28-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31888. 16 interactions.
DIPiDIP-956N.
MINTiMINT-4479766.

Proteomic databases

MaxQBiP46681.
PeptideAtlasiP46681.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL178W; YDL178W; YDL178W.
GeneIDi851376.
KEGGisce:YDL178W.

Organism-specific databases

EuPathDBiFungiDB:YDL178W.
SGDiS000002337. DLD2.

Phylogenomic databases

GeneTreeiENSGT00550000075086.
HOGENOMiHOG000230997.
InParanoidiP46681.
KOiK00102.
OMAiNEDWMRK.
OrthoDBiEOG7SJDDF.

Enzyme and pathway databases

BioCyciYEAST:YDL178W-MONOMER.
ReactomeiR-SCE-880009. Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.

Miscellaneous databases

NextBioi968507.
PROiP46681.

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. "AIP1, AIP2 and AIP3 encode novel components of the yeast actin cytoskeleton."
    Amberg D.C., Botstein D.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Signalling between mitochondria and the nucleus regulates the expression of a new D-lactate dehydrogenase activity in yeast."
    Chelstowska A., Liu Z., Jia Y., Amberg D., Butow R.A.
    Yeast 15:1377-1391(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Interaction of D-lactate dehydrogenase protein 2 (Dld2p) with F-actin: implication for an alternative function of Dld2p."
    Hachiya N.S., Sakasegawa Y., Jozuka A., Tsukita S., Kaneko K.
    Biochem. Biophys. Res. Commun. 319:78-82(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACTIN.

Entry informationi

Entry nameiDLD2_YEAST
AccessioniPrimary (citable) accession number: P46681
Secondary accession number(s): D6VRH4, Q66RH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, 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.