Reviewed,
UniProtKB/Swiss-Prot Q12627 (DLD1_KLULA)
Last modified
January 19, 2010.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: D-lactate dehydrogenase [cytochrome], mitochondrial EC=1.1.2.4 Alternative name(s): D-lactate ferricytochrome C oxidoreductase Short name=D-LCR | ||||||
| Gene names |
| ||||||
| Organism | Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome] | ||||||
| Taxonomic identifier | 28985 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces |
Protein attributes
| Sequence length | 576 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the stereospecific oxidation of D-lactate to pyruvate. |
| Catalytic activity | (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c. |
| Cofactor | Binds 2 FAD. Binds 4-6 zinc ions. |
| Subcellular location | |
| 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 Zinc |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | D-lactate dehydrogenase (cytochrome) activity Inferred from electronic annotation. Source: EC FAD bindingInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion | |||||||
| Chain | ? – 576 | D-lactate dehydrogenase [cytochrome], mitochondrial | PRO_0000020427 | ||||||
Regions | |||||||||
| Domain | 139 – 320 | 182 | FAD-binding PCMH-type | ||||||
Experimental info | |||||||||
| Sequence conflict | 539 | 1 | E → Q in CAA50635. Ref.1 | ||||||
| Sequence conflict | 564 | 1 | D → DKIF in CAA50635. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Carbon catabolite repression in Kluyveromyces lactis: isolation and characterization of the KIDLD gene encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase." Lodi T., O'Connor D., Goffrini P., Ferrero I. Mol. Gen. Genet. 244:622-629(1994) [PubMed: 7969031] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37. |
| [2] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L.Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X71628 Genomic DNA. Translation: CAA50635.1. CR382125 Genomic DNA. Translation: CAG99929.1. |
| PIR | S51528. |
| RefSeq | XP_454842.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q12627. |
Genome annotation databases | |
| GeneID | 2894285. |
| GenomeReviews | Gene locus KLLA0E19789g in contig CR382125_GR. |
| KEGG | kla:KLLA0E19789g. |
Phylogenomic databases | |
| eggNOG | fuNOG04541. |
| HOGENOM | HBG553036. |
| OMA | RDESHFI. |
| OrthoDB | EOG93N8VT. |
| PhylomeDB | Q12627. |
Enzyme and pathway databases | |
| BRENDA | 1.1.2.4. 74088. |
Family and domain databases | |
| InterPro | IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR016164. FAD-linked_Oxase-like_C. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR004113. FAD-linked_oxidase_C. IPR006094. Oxid_FAD_bind_N. [Graphical view] |
| Gene3D | G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 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... |
Entry information
| Entry name | DLD1_KLULA | ||||||||
| Accession | Primary (citable) accession number: Q12627 Secondary accession number(s): Q6CMJ7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

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