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P32891 (DLD1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-lactate dehydrogenase [cytochrome] 1, 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:YDL174C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 inner membrane Ref.4.

Induction

By D-lactate. Induced during respiratory adaptation.

Miscellaneous

Present with 10800 molecules/cell in log phase SD medium. Ref.5

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? – 587D-lactate dehydrogenase [cytochrome] 1, mitochondrialPRO_0000020428

Regions

Domain146 – 327182FAD-binding PCMH-type

Experimental info

Sequence conflict4391A → RR in CAA46852. Ref.1
Sequence conflict572 – 58716DKIFK…ANDYR → GQNL in CAA46852. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32891 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 07183BEAEEB2EB19

FASTA58765,293
        10         20         30         40         50         60 
MLWKRTCTRL IKPIAQPRGR LVRRSCYRYA STGTGSTDSS SQWLKYSVIA SSATLFGYLF 

        70         80         90        100        110        120 
AKNLYSRETK EDLIEKLEMV KKIDPVNSTL KLSSLDSPDY LHDPVKIDKV VEDLKQVLGN 

       130        140        150        160        170        180 
KPENYSDAKS DLDAHSDTYF NTHHPSPEQR PRIILFPHTT EEVSKILKIC HDNNMPVVPF 

       190        200        210        220        230        240 
SGGTSLEGHF LPTRIGDTIT VDLSKFMNNV VKFDKLDLDI TVQAGLPWED LNDYLSDHGL 

       250        260        270        280        290        300 
MFGCDPGPGA QIGGCIANSC SGTNAYRYGT MKENIINMTI VLPDGTIVKT KKRPRKSSAG 

       310        320        330        340        350        360 
YNLNGLFVGS EGTLGIVTEA TVKCHVKPKA ETVAVVSFDT IKDAAACASN LTQSGIHLNA 

       370        380        390        400        410        420 
MELLDENMMK LINASESTDR CDWVEKPTMF FKIGGRSPNI VNALVDEVKA VAQLNHCNSF 

       430        440        450        460        470        480 
QFAKDDDEKL ELWEARKVAL WSVLDADKSK DKSAKIWTTD VAVPVSQFDK VIHETKKDMQ 

       490        500        510        520        530        540 
ASKLINAIVG HAGDGNFHAF IVYRTPEEHE TCSQLVDRMV KRALNAEGTC TGEHGVGIGK 

       550        560        570        580 
REYLLEELGE APVDLMRKIK LAIDPKRIMN PDKIFKTDPN EPANDYR

« Hide

References

« Hide 'large scale' references
[1]"Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase."
Lodi T., Ferrero I.
Mol. Gen. Genet. 238:315-324(1993) [PubMed: 8492799] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[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. expand/collapse author list , 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]"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
Biochemistry 40:9758-9769(2001) [PubMed: 11502169] [Abstract]
Cited for: PROTEIN SEQUENCE OF 576-581, SUBCELLULAR LOCATION.
Strain: ATCC 201238 / W303-1B.
[5]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X66052 Genomic DNA. Translation: CAA46852.1.
Z67750 Genomic DNA. Translation: CAA91571.1.
Z74222 Genomic DNA. Translation: CAA98748.1.
BK006938 Genomic DNA. Translation: DAA11688.1.
PIRS61038.
RefSeqNP_010107.1. NM_001180234.1.

3D structure databases

ProteinModelPortalP32891.
SMRP32891. Positions 109-575.
ModBaseSearch...

Protein-protein interaction databases

IntActP32891. 15 interactions.
STRINGP32891.

2D gel databases

UCD-2DPAGEP32891.

Proteomic databases

PeptideAtlasP32891.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL174C; YDL174C; YDL174C.
GeneID851380.
KEGGsce:YDL174C.
NMPDRfig|4932.3.peg.841.

Organism-specific databases

CYGDYDL174c.
SGDS000002333. DLD1.

Phylogenomic databases

eggNOGfuNOG04541.
GeneTreeEFGT00050000001281.
HOGENOMHBG553036.
OrthoDBEOG4K6KCJ.

Gene expression databases

ArrayExpressP32891.
GenevestigatorP32891.
GermOnlineYDL174C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016166. 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]
Gene3DG3DSA: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.
KOK00102.
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...

Other

NextBio968519.

Entry information

Entry nameDLD1_YEAST
AccessionPrimary (citable) accession number: P32891
Secondary accession number(s): D6VRH8, Q12360
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: December 14, 2011
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

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