[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6386470 [NCBI, ExPASy, EBI, Israel, Japan] Campbell H.D., Rogers B.L., Young I.G.; "Nucleotide sequence of the respiratory D-lactate dehydrogenase gene of Escherichia coli."; Eur. J. Biochem. 144:367-373(1984).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-18. PubMed=3882663 [NCBI, ExPASy, EBI, Israel, Japan] Rule G.S., Pratt E.A., Chin C.C.Q., Wold F., Ho C.; "Overproduction and nucleotide sequence of the respiratory D-lactate dehydrogenase of Escherichia coli."; J. Bacteriol. 161:1059-1068(1985).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / BHB2600; Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K., Church G.M.; "Automated multiplex sequencing of the E.coli genome."; Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[6]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). DOI=10.1073/pnas.97.17.9413; PubMed=10944213 [NCBI, ExPASy, EBI, Israel, Japan] Dym O., Pratt E.A., Ho C., Eisenberg D.; "The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme."; Proc. Natl. Acad. Sci. U.S.A. 97:9413-9418(2000).

Comments

FUNCTION: First component of the membrane-bound D-lactate oxidase, which is believed to play an important role in the energization of the active transport of a variety of sugars and amino acids.
CATALYTIC ACTIVITY: (R)-lactate + NAD⁺ = pyruvate + NADH.
COFACTOR: FAD.
ENZYME REGULATION: Requires phospholipid for maximal activity.
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.

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

M10038; AAA23688.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X01067; CAA25531.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00007; AAA60530.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75194.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76610.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A21893; DEECDL.

RefSeq

AP_002730.1; -.
NP_416637.1; -.

3D structure databases

PDB

1F0X; X-ray; 1.90 A; A/B=1-571.

[ExPASy / RCSB / EBI]

PDBsum

1F0X; -.

ModBase

P06149.

Protein-protein interaction databases

IntAct

P06149; -.

Enzyme and pathway databases

BioCyc

EcoCyc:DLACTDEHYDROGFAD-MON; -.

2D gel databases

ECO2DBASE

H062.0; 6TH EDITION.

Organism-specific databases

EchoBASE

EB0227; -.

EcoGene

EG10231; dld.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR016172; D-lactate_DHase_C-sub1.
IPR016173; D-lactate_DHase_C-sub2.
IPR012256; D_lactate_DHase.
IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
IPR015409; Lactate_DHase_C.
IPR006094; Oxid_FAD_bind_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.70.610; D-lactate_dehydrogenase_C-sub1; 1.
G3DSA:3.30.1370.20; D-lactate_dehydrogenase_C-sub2; 1.
G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.

Pfam

PF01565; FAD_binding_4; 1.
PF09330; Lact-deh-memb; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000101; D-lactate_dh; 1.

PROSITE

PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P06149.

Genome annotation databases

GeneID

946653; -.

GenomeReviews

U00096_GR; b2133.
AP009048_GR; JW2121.

KEGG

ecj:JW2121; -.
eco:b2133; -.

Phylogenomic databases

HOGENOM

P06149; -.

Other

DrugBank

DB00756; Hexachlorophene.

Genome annotation databases

CMR

P06149; b2133.

Other

ProtoNet

P06149.

UniRef

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

Keywords

3D-structure; Cell membrane; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Membrane; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 571`	`570`	`D-lactate dehydrogenase.`	`PRO_0000079928`
`DOMAIN`	`42 213`	`172`	`FAD-binding PCMH-type.`
`HELIX`	`10 20`	`11`
`HELIX`	`22 24`	`3`
`HELIX`	`29 36`	`8`
`STRAND`	`39 41`	`3`
`STRAND`	`47 50`	`4`
`HELIX`	`55 67`	`13`
`STRAND`	`71 77`	`7`
`STRAND`	`81 83`	`3`
`STRAND`	`96 100`	`5`
`STRAND`	`107 110`	`4`
`TURN`	`111 114`	`4`
`STRAND`	`115 118`	`4`
`HELIX`	`124 131`	`8`
`HELIX`	`132 134`	`3`
`HELIX`	`143 147`	`5`
`HELIX`	`151 156`	`6`
`STRAND`	`174 179`	`6`
`STRAND`	`185 189`	`5`
`STRAND`	`191 193`	`3`
`HELIX`	`199 207`	`9`
`HELIX`	`213 215`	`3`
`HELIX`	`228 233`	`6`
`HELIX`	`247 249`	`3`
`STRAND`	`259 268`	`10`
`STRAND`	`277 284`	`8`
`HELIX`	`286 299`	`14`
`STRAND`	`305 311`	`7`
`HELIX`	`312 318`	`7`
`HELIX`	`379 387`	`9`
`STRAND`	`389 396`	`8`
`HELIX`	`400 414`	`15`
`STRAND`	`418 421`	`4`
`HELIX`	`424 434`	`11`
`HELIX`	`437 447`	`11`
`HELIX`	`449 451`	`3`
`STRAND`	`452 461`	`10`
`HELIX`	`475 478`	`4`
`STRAND`	`481 489`	`9`
`TURN`	`490 493`	`4`
`STRAND`	`494 502`	`9`
`HELIX`	`507 520`	`14`
`STRAND`	`527 529`	`3`
`TURN`	`532 534`	`3`
`HELIX`	`539 548`	`10`
`TURN`	`556 560`	`5`

Sequence information

Length: 571 AA [This is the length of the unprocessed precursor]

Molecular weight: 64612 Da [This is the MW of the unprocessed precursor]

CRC64: 77FB2C467CB4389F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSMTTTDNK AFLNELARLV GSSHLLTDPA KTARYRKGFR SGQGDALAVV FPGSLLELWR 

        70         80         90        100        110        120 
VLKACVTADK IILMQAANTG LTEGSTPNGN DYDRDVVIIS TLRLDKLHVL GKGEQVLAYP 

       130        140        150        160        170        180 
GTTLYSLEKA LKPLGREPHS VIGSSCIGAS VIGGICNNSG GSLVQRGPAY TEMSLFARIN 

       190        200        210        220        230        240 
EDGKLTLVNH LGIDLGETPE QILSKLDDDR IKDDDVRHDG RHAHDYDYVH RVRDIEADTP 

       250        260        270        280        290        300 
ARYNADPDRL FESSGCAGKL AVFAVRLDTF EAEKNQQVFY IGTNQPEVLT EIRRHILANF 

       310        320        330        340        350        360 
ENLPVAGEYM HRDIYDIAEK YGKDTFLMID KLGTDKMPFF FNLKGRTDAM LEKVKFFRPH 

       370        380        390        400        410        420 
FTDRAMQKFG HLFPSHLPPR MKNWRDKYEH HLLLKMAGDG VGEAKSWLVD YFKQAEGDFF 

       430        440        450        460        470        480 
VCTPEEGSKA FLHRFAAAGA AIRYQAVHSD EVEDILALDI ALRRNDTEWY EHLPPEIDSQ 

       490        500        510        520        530        540 
LVHKLYYGHF MCYVFHQDYI VKKGVDVHAL KEQMLELLQQ RGAQYPAEHN VGHLYKAPET 

       550        560        570 
LQKFYRENDP TNSMNPGIGK TSKRKNWQEV E

P06149 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