[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Muscle; PubMed=7937776 [NCBI, ExPASy, EBI, Israel, Japan] Tsuji S., Qureshi M.A., Hou E.W., Fitch W.M., Li S.S.-L.; "Evolutionary relationships of lactate dehydrogenases (LDHs) from mammals, birds, an amphibian, fish, barley, and bacteria: LDH cDNA sequences from Xenopus, pig, and rat."; Proc. Natl. Acad. Sci. U.S.A. 91:9392-9396(1994).
[2]	PROTEIN SEQUENCE OF 2-334. PubMed=838465 [NCBI, ExPASy, EBI, Israel, Japan] Kiltz H.-H., Keil W., Griesbach M., Petry K., Meyer H.; "The primary structure of porcine lactate dehydrogenase: isoenzymes M4 and H4."; Hoppe-Seyler's Z. Physiol. Chem. 358:123-127(1977).
[3]	SEQUENCE REVISION TO 22; 148; 216 AND 218. Kiltz H.-H.; Submitted (OCT-1977) to the PIR data bank.
[4]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). DOI=10.1016/0022-2836(81)90516-7; PubMed=7338899 [NCBI, ExPASy, EBI, Israel, Japan] Grau U.M., Trommer W.E., Rossmann M.G.; "Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7-A resolution."; J. Mol. Biol. 151:289-307(1981).

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

U07180; AAA50438.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A91671; DEPGLH.

NP_001106758.1; -.

3D structure databases

PDB

5LDH; X-ray; 2.70 A; A/B=2-334.

[ExPASy / RCSB / EBI]

PDBsum

5LDH; -.

ModBase

P00336.

Ontologies

GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001557; L-lactate/malate_DHase.
IPR011304; L-lactate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.110.10; lact_mal_DH; 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.

PS00064; L_LDH; 1.

Genome annotation databases

GeneID

407246; -.

KEGG

ssc:407246; -.

Phylogenomic databases

HOVERGEN

P00336; -.

Other

LinkHub

P00336; -.

UniRef

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

Keywords

3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 334`	`333`	`L-lactate dehydrogenase B chain.`	`PRO_0000168462`
`NP_BIND`	`30 58`	`29`	`NAD (By similarity).`
`ACT_SITE`	`194 194`		`Proton acceptor (By similarity).`
`BINDING`	`100 100`		`NAD (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`139 139`		`NAD or substrate (By similarity).`
`BINDING`	`170 170`		`Substrate (By similarity).`
`BINDING`	`249 249`		`Substrate (By similarity).`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MOD_RES`	`240 240`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`14 15`		`EE -> QQ (in Ref. 2; AA sequence).`
`CONFLICT`	`81 81`		`D -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`131 131`		`D -> N (in Ref. 2; AA sequence).`
`CONFLICT`	`214 214`		`E -> Q (in Ref. 2; AA sequence).`
`STRAND`	`24 26`	`3`
`HELIX`	`31 43`	`13`
`STRAND`	`49 51`	`3`
`HELIX`	`57 69`	`13`
`HELIX`	`70 72`	`3`
`HELIX`	`86 88`	`3`
`STRAND`	`92 95`	`4`
`TURN`	`98 99`	`2`
`TURN`	`107 108`	`2`
`HELIX`	`112 119`	`8`
`TURN`	`120 121`	`2`
`HELIX`	`122 128`	`7`
`STRAND`	`133 136`	`4`
`HELIX`	`141 152`	`12`
`HELIX`	`155 158`	`4`
`TURN`	`163 164`	`2`
`HELIX`	`165 179`	`15`
`TURN`	`215 218`	`4`
`HELIX`	`228 240`	`13`
`HELIX`	`247 266`	`20`
`TURN`	`267 267`	`1`
`STRAND`	`294 297`	`4`
`TURN`	`298 299`	`2`
`STRAND`	`300 304`	`5`
`HELIX`	`313 331`	`19`

Sequence information

Length: 334 AA [This is the length of the unprocessed precursor]

Molecular weight: 36612 Da [This is the MW of the unprocessed precursor]

CRC64: A0A2389BAB8FFD73 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATLKEKLIA PVAEEETTIP NNKITVVGVG QVGMACAISI LGKSLTDELA LVDVLEDKLK 

        70         80         90        100        110        120 
GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF 

       130        140        150        160        170        180 
IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG 

       190        200        210        220        230        240 
VHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY 

       250        260        270        280        290        300 
EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVQG MYGIENEVFL SLPCVLNARG 

       310        320        330 
LTSVINQKLK DDEVAQLKNS ADTLWGIQKD LKDL

P00336 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