Reviewed, UniProtKB/Swiss-Prot Q12627 (DLD1_KLULA)

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

Name:	DLD1
Synonyms:	DLD
Ordered Locus Names:	KLLA0E19789g

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	Mitochondrion matrix.
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 binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred 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

	Sequence		Length	Mass (Da)
	Q12627-1 [UniParc]. Last modified September 27, 2004. Version 2. Checksum: 629615C88758545F	FASTA	576	63,097
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 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

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	September 27, 2004
Last modified:	January 19, 2010
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)