P46681 (DLD2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-lactate dehydrogenase [cytochrome] 2, mitochondrial
EC=1.1.2.4

Alternative name(s):
Actin-interacting protein 2
D-lactate ferricytochrome C oxidoreductase
Short name=D-LCR

Gene names

Name:	DLD2
Synonyms:	AIP2
Ordered Locus Names:	YDL178W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [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.5
Catalytic activity	(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c.
Cofactor	FAD Potential.
Subunit structure	Interacts with F-actin. Ref.7
Subcellular location	Mitochondrion matrix Ref.5.
Miscellaneous	Present with 11400 molecules/cell in log phase SD medium. Ref.6
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 Reference proteome
Gene Ontology (GO)
Biological process	lactate metabolic process Traceable author statement Ref.5. Source: SGD
Cellular component	mitochondrial matrix Inferred from direct assay Ref.5. Source: SGD
Molecular function	D-lactate dehydrogenase (cytochrome) activity Inferred from direct assay Ref.5. Source: SGD UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro actin binding Inferred from mutant phenotype. Source: SGD 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 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.4

Sequences

	Sequence		Length	Mass (Da)
	P46681 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 42FDFBE5CA7E11B7	FASTA	530	59,268
	10 20 30 40 50 60 MLRNILVRST GSNFKFAGRY MKSSALLGYY RRVNYYSTKI QTRLTSENYP DVHRDPRFKK 70 80 90 100 110 120 LTSDDLNYFK SILSEQEILR ASESEDLSFY NEDWMRKYKG QSKLVLRPKS VEKVSLILNY 130 140 150 160 170 180 CNDEKIAVVP QGGNTGLVGG SVPIFDELIL SLANLNKIRD FDPVSGILKC DAGVILENAN 190 200 210 220 230 240 NYVMEQNYMF PLDLGAKGSC HVGGVVATNA GGLRLLRYGS LHGSVLGLEV VMPNGQIVNS 250 260 270 280 290 300 MHSMRKDNTG YDLKQLFIGS EGTIGIITGV SILTVPKPKA FNVSYLSVES FEDVQKVFVR 310 320 330 340 350 360 ARQELSEILS AFEFMDAKSQ VLAKSQLKDA AFPLEDEHPF YILIETSGSN KDHDDSKLET 370 380 390 400 410 420 FLENVMEEGI VTDGVVAQDE TELQNLWKWR EMIPEASQAN GGVYKYDVSL PLKDLYSLVE 430 440 450 460 470 480 ATNARLSEAE LVGDSPKPVV GAIGYGHVGD GNLHLNVAVR EYNKNIEKTL EPFVYEFVSS 490 500 510 520 530 KHGSVSAEHG LGFQKKNYIG YSKSPEEVKM MKDLKVHYDP NGILNPYKYI

References

	« Hide 'large scale' referencesShow '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. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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.
[6]	"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].
[7]	"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. BK006938 Genomic DNA. Translation: DAA11684.1.
PIR	S61034.
RefSeq	NP_010103.1. NM_001180238.1.
3D structure databases
ProteinModelPortal	P46681.
SMR	P46681. Positions 60-530.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-956N.
STRING	P46681.
Proteomic databases
PeptideAtlas	P46681.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL178W; YDL178W; YDL178W.
GeneID	851376.
KEGG	sce:YDL178W.
NMPDR	fig|4932.3.peg.837.
Organism-specific databases
CYGD	YDL178w.
SGD	S000002337. DLD2.
Phylogenomic databases
eggNOG	fuNOG04802.
GeneTree	EFGT00050000001281.
HOGENOM	HBG553036.
OMA	EPFVYEW.
OrthoDB	EOG4F4WKV.
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. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR004113. FAD-linked_oxidase_C. IPR006094. Oxid_FAD_bind_N. IPR016171. Vanillyl_alc_oxidase_C-sub2. [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. G3DSA:1.10.45.10. Vanillyl_alc_oxidase_C-sub2. 1 hit.
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...
Other
NextBio	968507.

Entry information

Entry name

DLD2_YEAST

Accession

Primary (citable) accession number: P46681
Secondary accession number(s): D6VRH4, Q66RH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program