Q12627 (DLD1_KLULA) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces › Kluyveromyces lactis

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 + 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.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	D-lactate dehydrogenase (cytochrome) activity Inferred from electronic annotation. Source: EC UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
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 [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] [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. , 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.
PIR	S51528.
RefSeq	XP_454842.1. XM_454842.1.
3D structure databases
ProteinModelPortal	Q12627.
ModBase	Search...
Protein-protein interaction databases
STRING	28985.Q12627.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2894285.
KEGG	kla:KLLA0E19691g.
Phylogenomic databases
eggNOG	COG0277.
HOGENOM	HOG000230995.
KO	K00102.
OMA	VAILIDP.
OrthoDB	EOG4K6KCJ.
Family and domain databases
Gene3D	1.10.45.10. 1 hit. 3.30.43.10. 1 hit. 3.30.465.10. 1 hit.
InterPro	IPR016169. 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]
Pfam	PF02913. FAD-oxidase_C. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
SUPFAM	SSF55103. FAD-binding_2. 1 hit. SSF56176. FAD-binding_2. 1 hit.
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:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program