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Reviewed, UniProtKB/Swiss-Prot P26298 (LDHD_LACPE)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismLactobacillus pentosus
Taxonomic identifier1589 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer.

Miscellaneous

Also active on D-glycerate.

Sequence similarities

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

Caution

Was originally (Ref.1) thought to originate from L.plantarum.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionD-lactate dehydrogenase activity

Inferred from electronic annotation. Source: EC

NAD or NADH binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332D-lactate dehydrogenase
PRO_0000075956

Sites

Active site2351
Active site2641
Active site2961Proton donor

Sequences

Sequence LengthMass (Da)Tools
P26298-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: FA63723C63B53EBE

FASTA33237,183
        10         20         30         40         50         60 
MKIIAYAVRD DERPFFDTWM KENPDVEVKL VPELLTEDNV DLAKGFDGAD VYQQKDYTAE 

        70         80         90        100        110        120 
VLNKLADEGV KNISLRNVGV DNLDVPTVKA RGLNISNVPA YSPNAIAELS VTQLMQLLRQ 

       130        140        150        160        170        180 
TPMFNKKLAK QDFRWAPDIA KELNTMTVGV IGTGRIGRAA IDIFKGFGAK VIGYDVYRNA 

       190        200        210        220        230        240 
ELEKEGMYVD TLDELYAQAD VITLHVPALK DNYHMLNADA FSKMKDGAYI LNFARGTLID 

       250        260        270        280        290        300 
SEDLIKALDS GKVAGAALVT YEYETKIFNK DLEGQTIDDK VFMNLFNRDN VLITPHTAFY 

       310        320        330 
TETAVHNMVH VSMNSNKQFI ETGKADTQVK FD 

« Hide

References

[1]"D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum."
Ohta T., Taguchi H.
J. Biol. Chem. 266:12588-12594(1991) [PubMed: 1840590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 8041 / DSM 20314 / JCM 1558 / NCDO 363 / NCIMB 8026.
[2]"Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase."
Stoll V.S., Kimber M.S., Pai E.F.
Structure 4:437-447(1996) [PubMed: 8740366] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Cross-references

Sequence databases

D90339 Genomic DNA. Translation: BAA14352.1.
PIRA40885.

3D structure databases

HSSPHSSP built from PDB template 1J4A based on UniProtKB P26297.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.28. 1616.

Family and domain databases

InterProIPR006139. D-isomer_2_OHA_DH.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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...

Entry information

Entry nameLDHD_LACPE
AccessionPrimary (citable) accession number: P26298
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents