NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

Comments

CATALYTIC ACTIVITY: (R)-lactate + NAD⁺ = pyruvate + NADH.
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

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

BA000033; BAB96309.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_647261.1; -.

3D structure databases

HSSP

P26297; 1J49. [HSSP ENTRY / PDB]

ModBase

Q8NUT2.

Enzyme and pathway databases

BioCyc

SAUR196620:MW2444-MON; -.

Ontologies

GO:0008720;	Molecular function: D-lactate dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

Genome annotation databases

GeneID

1004580; -.

GenomeReviews

BA000033_GR; MW2444.

KEGG

sam:MW2444; -.

Phylogenomic databases

HOGENOM

Q8NUT2; -.

Genome annotation databases

CMR

Q8NUT2; MW2444.

Other

UniRef

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

Keywords

Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 330`	`330`	`D-lactate dehydrogenase.`	`PRO_0000075965`
`ACT_SITE`	`235 235`		`By similarity.`
`ACT_SITE`	`264 264`		`By similarity.`
`ACT_SITE`	`296 296`		`Proton donor (By similarity).`

Sequence information

Length: 330 AA [This is the length of the unprocessed precursor]

Molecular weight: 36713 Da [This is the MW of the unprocessed precursor]

CRC64: 1303A04AD0EE022F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKIMFFGTR DYEKEMALNW GKKNNVEVTT SKELLSSATV DQLKDYDGVT TMQFGKLEDD 

        70         80         90        100        110        120 
VYPKLESYGI KQIAQRTAGF DMYDLDLAKK HNIVISNVPS YSPETIAEYS VSIALQLVRR 

       130        140        150        160        170        180 
FPDIERRVQA HDFTWQAEIM SKPVKNMTVA IIGTGRIGAA TAKIYAGFGA TITAYDAYPN 

       190        200        210        220        230        240 
KDLDFLTYKD SVKEAIKDAD IISLHVPANK ESYHLFDKAM FDHVKKGAIL VNAARGAVIN 

       250        260        270        280        290        300 
TPDLIAAVND GTLLGAAIDT YENEAAYFTN DWTNKDIDDK TLLELIEHER ILVTPHIAFF 

       310        320        330 
SDEAVQNLVE GGLNAALSVI NTSTCETRLN

Q8NUT2 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