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Q12627 (DLD1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
Name:DLD1
Synonyms:DLD
Ordered Locus Names:KLLA0E19789g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 + 2 H+.

Cofactor

Binds 2 FAD.

Binds 4-6 zinc ions.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the FAD-binding oxidoreductase/transferase type 4 family.

Contains 1 FAD-binding PCMH-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 576D-lactate dehydrogenase [cytochrome], mitochondrialPRO_0000020427

Regions

Domain139 – 320182FAD-binding PCMH-type

Experimental info

Sequence conflict5391E → Q in CAA50635. Ref.1
Sequence conflict5641D → DKIF in CAA50635. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q12627 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: 629615C88758545F

FASTA57663,097
        10         20         30         40         50         60 
MFRFVGRSGF ALRGSLQLRK DVLRSRTTAV AKRHYSSSNG NNGGGFSSAI LSVLGGSLIG 

        70         80         90        100        110        120 
GGFVAYALGS QFEKEKSVSD LSIARLEDLD SPEYCDKETF AKALVELKDV LENDPENFTV 

       130        140        150        160        170        180 
AKDDLDAHSD TYFNSHHAEA NQRPEIVLYP RNTEDVSKLL KICHKYSIPV IPFSGGTSLE 

       190        200        210        220        230        240 
GHFLPTRPGS CVVLDISKYL NKIIQLNKED LDVVVQGGVP WEELNEYLND HGLLFGCDPG 

       250        260        270        280        290        300 
PGAQIAGCIA NSCSGTNAYR YGTMKENVVN ITMCMADGTI VKTKRRPRKS SAGYNLNGLI 

       310        320        330        340        350        360 
IGSEGTLGIV TEATIKCHVR STFETVAVVP FPTVSDAASC SSHLIQAGIQ LNAMELLDDN 

       370        380        390        400        410        420 
MMKIINQSGA TSKDNWVESP TLFFKIGGRS EQIIQEVIKE VEKIASQHNN TKFEFATDED 

       430        440        450        460        470        480 
SKLELWEARK VALWSTIDTG RKTNPDANIW TTDVAVPISK FADVINATKE EMNASGLLTS 

       490        500        510        520        530        540 
LVGHAGDGNF HAFIIYNTEQ RKTAETIVEN MVKRAIDAEG TCTGEHGVGI GKRDYLLEEV 

       550        560        570 
GEDTVAVMRK LKLALDPKRI LNPDKIFKID PNDHQH 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / 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. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71628 Genomic DNA. Translation: CAA50635.1.
CR382125 Genomic DNA. Translation: CAG99929.1.
PIRS51528.
RefSeqXP_454842.1. XM_454842.1.

3D structure databases

ProteinModelPortalQ12627.
ModBaseSearch...

Protein-protein interaction databases

STRING28985.Q12627.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2894285.
KEGGkla:KLLA0E19691g.

Phylogenomic databases

eggNOGCOG0277.
HOGENOMHOG000230995.
KOK00102.
OMAVAILIDP.
OrthoDBEOG4K6KCJ.

Family and domain databases

Gene3D1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProIPR016169. 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]
PfamPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. FAD-binding_2. 1 hit.
SSF56176. FAD-binding_2. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDLD1_KLULA
AccessionPrimary (citable) accession number: Q12627
Secondary accession number(s): Q6CMJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 27, 2004
Last modified: May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families