[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ML1; PubMed=8081494 [NCBI, ExPASy, EBI, Israel, Japan] Swindell S.R., Griffin H.G., Gasson M.J.; "Cloning, sequencing and comparison of three lactococcal L-lactate dehydrogenase genes."; Microbiology 140:1301-1305(1994).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=AM4, AM5, CM1-3, and MSUA2; PubMed=9023947 [NCBI, ExPASy, EBI, Israel, Japan] Urbach E., Daniels B., Salama M.S., Sandine W.E., Giovannoni S.J.; "The ldh phylogeny for environmental isolates of Lactococcus lactis is consistent with rRNA genotypes but not with phenotypes."; Appl. Environ. Microbiol. 63:694-702(1997).
[3]	PROTEIN SEQUENCE OF 2-22 AND 247-298. STRAIN=US3; DOI=10.1016/0005-2795(79)90254-X; PubMed=518918 [NCBI, ExPASy, EBI, Israel, Japan] Crossley L.G., Jago G.R., Davidson B.E.; "Partial sequence data for the L-(+)-lactate dehydrogenase from Streptococcus cremoris US3 including the amino acid sequences around the single cysteine residue and at the N-terminus."; Biochim. Biophys. Acta 581:342-355(1979).

Comments

CATALYTIC ACTIVITY: (S)-lactate + NAD⁺ = pyruvate + NADH.
PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
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

U02385; AAA61961.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U78630; AAB51674.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U78631; AAB51675.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U78633; AAB51677.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U78635; AAB51679.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A20629; A20629.

3D structure databases

HSSP

P00343; 1LLC. [HSSP ENTRY / PDB]

ModBase

P04034.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
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).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

TIGRFAMs

TIGR01771; L-LDH-NAD; 1.

PS00064; L_LDH; 1.

Other

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

Keywords

Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 325`	`324`	`L-lactate dehydrogenase 1.`	`PRO_0000168354`
`NP_BIND`	`15 43`	`29`	`NAD (By similarity).`
`ACT_SITE`	`178 178`		`Proton acceptor (By similarity).`
`BINDING`	`91 91`		`Substrate (By similarity).`
`BINDING`	`123 123`		`NAD or substrate (By similarity).`
`BINDING`	`154 154`		`Substrate (By similarity).`
`BINDING`	`232 232`		`Substrate (By similarity).`
`MOD_RES`	`223 223`		`Phosphotyrosine (By similarity).`
`VARIANT`	`127 127`	`1`	`I -> T (in strain: CM1-3).`
`VARIANT`	`213 213`	`1`	`K -> E (in strain: AM4 and CM1-3).`
`VARIANT`	`293 293`	`1`	`D -> E (in strain: AM4).`
`CONFLICT`	`5 5`		`Q -> E (in Ref. 3; AA sequence).`
`CONFLICT`	`20 20`		`S -> A (in Ref. 3; AA sequence).`

Sequence information

Length: 325 AA [This is the length of the unprocessed precursor]

Molecular weight: 35050 Da [This is the MW of the unprocessed precursor]

CRC64: 6F50D8343AF13AA9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADKQRKKVI LVGDGAVGSS YAFALVNQGI AQELGIVDLF KEKTQGDAED LSHALAFTSP 

        70         80         90        100        110        120 
KKIYSADYSD ASDADLVVLT SGAPQKPGET RLDLVEKNLR ITKDVVTKIV ASGFKGIFLV 

       130        140        150        160        170        180 
AANPVDILTY ATWKFSGFPK NRVVGSGTSL DTARFRQALA EKVDVDARSI HAYIMGEHGD 

       190        200        210        220        230        240 
SEFAVWSHAN VAGVKLEQWF QENDYLNEAE IVKLFESVRD AAYSIIAKKG ATFYGVAVAL 

       250        260        270        280        290        300 
ARITKAILDD EHAVLPVSVF QDGQYGVSDC YLGQPAVVGA EGVVNPIHIP LNDAEMQKME 

       310        320 
ASGAQLKAII DEAFAKEEFA SAVKN

P04034 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