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P26297 (LDHD_LACDA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. 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

Names and origin

Protein namesRecommended name:
D-lactate dehydrogenase

Short name=D-LDH
EC=1.1.1.28
Alternative name(s):
D-specific D-2-hydroxyacid dehydrogenase
Gene names
Name:ldhA
Ordered Locus Names:Ldb0101
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [Complete proteome] [HAMAP]
Taxonomic identifier390333 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(R)-lactate + NAD+ = pyruvate + NADH.

Subunit structure

Homodimer. Ref.8

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functionD-lactate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NAD binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 333332D-lactate dehydrogenase
PRO_0000075953

Regions

Nucleotide binding153 – 17927NADH
Nucleotide binding156 – 1572NAD By similarity
Nucleotide binding234 – 2363NAD By similarity
Nucleotide binding297 – 3004NAD By similarity

Sites

Active site2361
Active site2651
Active site2971Proton donor
Binding site2601NAD By similarity

Experimental info

Mutagenesis2061H → Q: Increase of activity. Ref.6
Mutagenesis2361R → K: Decrease of activity. Ref.6
Mutagenesis2601D → N: Decrease of activity. Ref.6
Mutagenesis2651E → Q: Decrease of activity. Ref.6
Mutagenesis2971H → Q: 90% loss of activity. Ref.6
Sequence conflict411V → A in AAA25246. Ref.2
Sequence conflict1171R → A in CAA42781. Ref.1
Sequence conflict1221D → A in AAA25246. Ref.2
Sequence conflict1521I → V in AAA25246. Ref.2
Sequence conflict1741A → T in CAA42781. Ref.1
Sequence conflict2201E → K in AAA25246. Ref.2
Sequence conflict2541I → V in AAA25246. Ref.2
Sequence conflict2681I → V in AAA25246. Ref.2
Sequence conflict2731W → R in AAA25246. Ref.2

Secondary structure

............................................................ 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26297 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 16E8B68D54B9D9D4

FASTA33337,049
        10         20         30         40         50         60 
MTKIFAYAIR EDEKPFLKEW EDAHKDVEVE YTDKLLTPET VALAKGADGV VVYQQLDYTA 

        70         80         90        100        110        120 
ETLQALADNG ITKMSLRNVG VDNIDMAKAK ELGFQITNVP VYSPNAIAEH AAIQAARILR 

       130        140        150        160        170        180 
QDKAMDEKVA RHDLRWAPTI GREVRDQVVG VIGTGHIGQV FMQIMEGFGA KVIAYDIFRN 

       190        200        210        220        230        240 
PELEKKGYYV DSLDDLYKQA DVISLHVPDV PANVHMINDE SIAKMKQDVV IVNVSRGPLV 

       250        260        270        280        290        300 
DTDAVIRGLD SGKIFGYAMD VYEGEVGIFN EDWEGKEFPD ARLADLIARP NVLVTPHTAF 

       310        320        330 
YTTHAVRNMV VKAFDNNLEL VEGKEAETPV KVG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the D-lactate dehydrogenase gene from Lactobacillus delbrueckii subsp. bulgaricus by complementation in Escherichia coli."
Bernard N., Ferain T., Garmyn D., Hols P., Delcour J.
FEBS Lett. 290:61-64(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Primary structure, physicochemical properties, and chemical modification of NAD(+)-dependent D-lactate dehydrogenase. Evidence for the presence of Arg-235, His-303, Tyr-101, and Trp-19 at or near the active site."
Kochhar S., Hunziker P., Leong-Morgenthaler P.M., Hottinger H.
J. Biol. Chem. 267:8499-8513(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[3]"Cloning and overexpression of the Lactobacillus bulgaricus NAD(+)-dependent D-lactate dehydrogenase gene in Escherichia coli: purification and characterization of the recombinant enzyme."
Kochhar S., Chuard N., Hottinger H.
Biochem. Biophys. Res. Commun. 185:705-712(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution."
van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. expand/collapse author list , Weissenbach J., Ehrlich S.D., Maguin E.
Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11842 / DSM 20081.
[5]"Evolutionary relationship of NAD(+)-dependent D-lactate dehydrogenase: comparison of primary structure of 2-hydroxy acid dehydrogenases."
Kochhar S., Hunziker P., Leong-Morgenthaler P.M., Hottinger H.
Biochem. Biophys. Res. Commun. 184:60-66(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO OTHER ENZYMES OF THIS FAMILY.
[6]"D-2-hydroxy-4-methylvalerate dehydrogenase from Lactobacillus delbrueckii subsp. bulgaricus. II. Mutagenic analysis of catalytically important residues."
Bernard N., Johnsen K., Gelpi J.L., Alvarez J.A., Ferain T., Garmyn D., Hols P., Cortes A., Clarke A.R., Holbrook J.J., Delcour J.
Eur. J. Biochem. 244:213-219(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-206; ARG-236; ASP-260; GLU-265 AND HIS-297.
[7]"Prediction of structurally conserved regions of D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase."
Vinals C., Depiereux E., Feytmans E.
Biochem. Biophys. Res. Commun. 192:182-188(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[8]"Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus."
Razeto A., Kochhar S., Hottinger H., Dauter M., Wilson K.S., Lamzin V.S.
J. Mol. Biol. 318:109-119(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADH, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60220 Genomic DNA. Translation: CAA42781.1.
M85224 Genomic DNA. Translation: AAA25246.1.
CR954253 Genomic DNA. Translation: CAI96942.1.
PIRA38094.
RefSeqYP_618304.1. NC_008054.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DLDmodel-A1-333[»]
1J49X-ray2.20A/B1-333[»]
1J4AX-ray1.90A/B/C/D1-333[»]
ProteinModelPortalP26297.
SMRP26297. Positions 1-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390333.Ldb0101.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI96942; CAI96942; Ldb0101.
GeneID4085369.
KEGGldb:Ldb0101.
PATRIC22215856. VBILacDel123523_0087.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1052.
HOGENOMHOG000136695.
KOK03778.
OMAFMQIMEG.
OrthoDBEOG61VZ8G.
ProtClustDBCLSK912466.

Enzyme and pathway databases

BioCycLDEL390333:GIXG-99-MONOMER.
SABIO-RKP26297.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26297.

Entry information

Entry nameLDHD_LACDA
AccessionPrimary (citable) accession number: P26297
Secondary accession number(s): Q1G7V7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references