[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=DG301; PubMed=8300514 [NCBI, ExPASy, EBI, Israel, Japan] Ferain T., Garmyn D., Bernard N., Hols P., Delcour J.; "Lactobacillus plantarum ldhL gene: overexpression and deletion."; J. Bacteriol. 176:596-601(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=L137; Kim J., Tsutsui M., Yamashita M., Murooka Y.; "Expression of Derf 7 gene in Lactobacillus plantarum."; Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1; DOI=10.1073/pnas.0337704100; PubMed=12566566 [NCBI, ExPASy, EBI, Israel, Japan] Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J.; "Complete genome sequence of Lactobacillus plantarum WCFS1."; Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-320. Ham J., Kim H., Kim H.; "Expression of LDH gene in Candida kefyr isolated from Mongolian Koumiss."; Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: (S)-lactate + NAD⁺ = pyruvate + NADH.
PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1 .
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the LDH/MDH superfamily. LDH 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

X70926; CAA50277.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB177763; BAD16691.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL935253; CAD63155.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF548372; AAN40797.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A36957; A36957.

RefSeq

NP_784314.1; -.

3D structure databases

HSSP

P56511; 1EZ4. [HSSP ENTRY / PDB]

SMR

P56512; 3-320.

ModBase

P56512.

Enzyme and pathway databases

BioCyc

LPLA220668:LP_0537-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004459;	Molecular function: L-lactate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0019642;	Biological process: anaerobic glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00488; -; 1.
PBIL [Tree]

InterPro

IPR001557; L-lactate/malate_DHase.
IPR011304; L-lactate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.110.10; lact_mal_DH; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000102; Lac_mal_DH; 1.

PRINTS

PR00086; LLDHDRGNASE.

TIGRFAMs

TIGR01771; L-LDH-NAD; 1.

PROSITE

PS00064; L_LDH; 1.

BLOCKS

P56512.

Genome annotation databases

GeneID

1061886; -.

GenomeReviews

AL935263_GR; lp_0537.

KEGG

lpl:lp_0537; -.

NMPDR

fig|220668.1.peg.448; -.

Phylogenomic databases

HOGENOM

P56512; -.

Genome annotation databases

CMR

P56512; lp_0537.

Other

ProtoNet

P56512.

UniRef

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

Keywords

Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 320`	`320`	`L-lactate dehydrogenase 1.`	`PRO_0000168357`
`NP_BIND`	`16 44`	`29`	`NAD (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor (By similarity).`
`BINDING`	`92 92`		`Substrate (By similarity).`
`BINDING`	`124 124`		`NAD or substrate (By similarity).`
`BINDING`	`155 155`		`Substrate (By similarity).`
`BINDING`	`232 232`		`Substrate (By similarity).`
`MOD_RES`	`223 223`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`54 54`		`D -> H (in Ref. 1; CAA50277).`
`CONFLICT`	`245 245`		`K -> Q (in Ref. 2; BAD16691).`
`CONFLICT`	`302 302`		`S -> C (in Ref. 1; CAA50277).`

Sequence information

Length: 320 AA [This is the length of the unprocessed precursor]

Molecular weight: 34206 Da [This is the MW of the unprocessed precursor]

CRC64: 34B8A5FD12A64EBC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSMPNHQKV VLVGDGAVGS SYAFAMAQQG IAEEFVIVDV VKDRTKGDAL DLEDAQAFTA 

        70         80         90        100        110        120 
PKKIYSGEYS DCKDADLVVI TAGAPQKPGE SRLDLVNKNL NILSSIVKPV VDSGFDGIFL 

       130        140        150        160        170        180 
VAANPVDILT YATWKFSGFP KDRVIGSGTS LDSSRLRVAL GKQFNVDPRS VDAYIMGEHG 

       190        200        210        220        230        240 
DSEFAAYSTA TIGTRPVRDV AKEQGVSDED LAKLEDGVRN KAYDIINLKG ATFYGIGTAL 

       250        260        270        280        290        300 
MRISKAILRD ENAVLPVGAY MDGQYGLNDI YIGTPAVIGG TGLKQIIESP LSADELKKMQ 

       310        320 
DSAATLKKVL NDGLAELENK

P56512 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