NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 8041 / DSM 20314 / JCM 1558 / NCDO 363 / NCIMB 8026;
PubMed=1840590 [NCBI, ExPASy, EBI, Israel, Japan]
Ohta T., Taguchi H.;
"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.";
J. Biol. Chem. 266:12588-12594(1991).

[2]

X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1016/S0969-2126(96)00049-4; PubMed=8740366 [NCBI, ExPASy, EBI, Israel, Japan]
Stoll V.S., Kimber M.S., Pai E.F.;
"Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase.";
Structure 4:437-447(1996).

Comments

CATALYTIC ACTIVITY: (R)-lactate + NAD⁺ = pyruvate + NADH.
SUBUNIT: Homodimer.
MISCELLANEOUS: Also active on D-glycerate.
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
CAUTION: Was originally (PubMed:1840590) thought to originate from L.plantarum.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D90339; BAA14352.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A40885; A40885.

3D structure databases

HSSP

P26297; 1J4A. [HSSP ENTRY / PDB]

ModBase

P26298.

Family and domain databases

InterPro

IPR006139; D-isomer_2_OHA_DHase.
IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00389; 2-Hacid_dh; 1.
PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.

PROSITE

PS00065; D_2_HYDROXYACID_DH_1; 1.
PS00670; D_2_HYDROXYACID_DH_2; 1.
PS00671; D_2_HYDROXYACID_DH_3; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 332`	`332`	`D-lactate dehydrogenase.`	`PRO_0000075956`
`ACT_SITE`	`235 235`
`ACT_SITE`	`264 264`
`ACT_SITE`	`296 296`		`Proton donor.`

Sequence information

Length: 332 AA [This is the length of the unprocessed precursor]

Molecular weight: 37183 Da [This is the MW of the unprocessed precursor]

CRC64: FA63723C63B53EBE [This is a checksum on the sequence]

        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

P26298 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools