Reviewed,
UniProtKB/Swiss-Prot P46681 (DLD2_YEAST)
Last modified
January 19, 2010.
Version 77.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: D-lactate dehydrogenase [cytochrome] 2, mitochondrial EC=1.1.2.4 Alternative name(s): D-lactate ferricytochrome C oxidoreductase Short name=D-LCR Actin-interacting protein 2 | ||||||
| Gene names |
| ||||||
| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 530 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | In addition to its enzymatic role it could play an important role in the yeast cell morphology. Ref.4 |
| Catalytic activity | (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c. |
| Cofactor | FAD Potential. |
| Subunit structure | Interacts with F-actin. Ref.6 |
| Subcellular location | |
| Miscellaneous | Present with 11400 molecules/cell in log phase SD medium. Ref.5 |
| Sequence similarities | Belongs to the FAD-binding oxidoreductase/transferase type 4 family. Contains 1 FAD-binding PCMH-type domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lactate metabolic process Ref.4 Traceable author statement. Source: SGD oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Ref.4 Inferred from direct assay. Source: SGD |
| Molecular function | D-lactate dehydrogenase (cytochrome) activity Ref.4 Inferred from direct assay. Source: SGD FAD bindingInferred from electronic annotation. Source: InterPro actin binding Ref.6Inferred from mutant phenotype. Source: SGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 530 | D-lactate dehydrogenase [cytochrome] 2, mitochondrial | PRO_0000020429 | ||||||
Regions | |||||||||
| Domain | 98 – 277 | 180 | FAD-binding PCMH-type | ||||||
Experimental info | |||||||||
| Sequence conflict | 239 | 1 | N → S in AAU09682. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. Zaccaria P.Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [3] | "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J.Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [4] | "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: 10509019] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. |
| [5] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [6] | "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: 15158445] [Abstract] Cited for: INTERACTION WITH ACTIN. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U35667 Genomic DNA. Translation: AAA79142.1. Z67750 Genomic DNA. Translation: CAA91567.1. Z74226 Genomic DNA. Translation: CAA98752.1. AY723765 Genomic DNA. Translation: AAU09682.1. |
| PIR | S61034. |
| RefSeq | NP_010103.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-956N. |
| STRING | P46681. |
Proteomic databases | |
| PeptideAtlas | P46681. |
Genome annotation databases | |
| Ensembl | YDL178W; YDL178W; YDL178W; Saccharomyces cerevisiae. [Genome view] |
| GeneID | 851376. |
| KEGG | sce:YDL178W. |
| NMPDR | fig|4932.3.peg.837. |
Organism-specific databases | |
| CYGD | YDL178w. |
| SGD | S000002337. DLD2. |
Phylogenomic databases | |
| eggNOG | fuNOG04802. |
| HOGENOM | HBG553036. |
| OMA | LKYCNER. |
| OrthoDB | EOG93N8VT. |
| PhylomeDB | P46681. |
Enzyme and pathway databases | |
| BRENDA | 1.1.2.4. 250. |
Gene expression databases | |
| ArrayExpress | P46681. |
| Genevestigator | P46681. |
| GermOnline | YDL178W. Saccharomyces cerevisiae. |
Family and domain databases | |
| InterPro | 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. [Graphical view] |
| Gene3D | G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. |
| Pfam | PF02913. FAD-oxidase_C. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view] |
| PROSITE | PS51387. FAD_PCMH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 968507. |
Entry information
| Entry name | DLD2_YEAST | ||||||||
| Accession | Primary (citable) accession number: P46681 Secondary accession number(s): Q66RH8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


