[1]	PROTEIN SEQUENCE. STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924; PubMed=6352452 [NCBI, ExPASy, EBI, Israel, Japan] Wirz B., Suter F., Zuber H.; "Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. III) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Hydroxylamine-, o-iodosobenzoic acid- and tryptic-fragments. The complete amino-acid sequence."; Hoppe-Seyler's Z. Physiol. Chem. 364:893-909(1983).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(86)90165-4; PubMed=3026926 [NCBI, ExPASy, EBI, Israel, Japan] Barstow D.A., Clarke A.R., Chia W.N., Wigley D., Sharman A.F., Holbrook J.J., Atkinson T., Minton N.P.; "Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilus L-lactate dehydrogenase gene."; Gene 46:47-55(1986).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3675869 [NCBI, ExPASy, EBI, Israel, Japan] Zuelli F., Weber H., Zuber H.; "Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, VI. Nucleotide sequences of lactate dehydrogenase genes from the thermophilic bacteria Bacillus stearothermophilus, B. caldolyticus and B. caldotenax."; Biol. Chem. Hoppe-Seyler 368:1167-1177(1987).
[4]	PARTIAL PROTEIN SEQUENCE. STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924; PubMed=6618448 [NCBI, ExPASy, EBI, Israel, Japan] Tratschin J.D., Wirz B., Frank G., Zuber H.; "Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria. II) The primary structure of thermophilic lactate dehydrogenase from Bacillus stearothermophilus. Cyanogen bromide fragments and partial sequence."; Hoppe-Seyler's Z. Physiol. Chem. 364:879-892(1983).
[5]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE ANALOG. DOI=10.1016/0022-2836(92)90733-Z; PubMed=1731077 [NCBI, ExPASy, EBI, Israel, Japan] Wigley D.B., Gamblin S.J., Turkenburg J.P., Dodson E.J., Piontek K., Muirhead H., Holbrook J.J.; "Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5-A resolution."; J. Mol. Biol. 223:317-335(1992).

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

M14788; AAA22568.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19396; AAA22567.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A26053; DEBSLF.

3D structure databases

PDB

1LDB; X-ray; 2.80 A; A/B/C/D=1-317.	[ExPASy / RCSB / EBI]
1LDN; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-316.	[ExPASy / RCSB / EBI]
2LDB; X-ray; 3.00 A; A/B/C/D=1-317.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1LDB; -.
1LDN; -.
2LDB; -.

ModBase

P00344.

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).
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.

PRINTS

PR00086; LLDHDRGNASE.

TIGRFAMs

TIGR01771; L-LDH-NAD; 1.

PS00064; L_LDH; 1.

Other

P00344; -.

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 317`	`317`	`L-lactate dehydrogenase.`	`PRO_0000168328`
`NP_BIND`	`15 43`	`29`	`NAD (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor.`
`BINDING`	`92 92`		`Substrate.`
`BINDING`	`124 124`		`NAD or substrate.`
`BINDING`	`155 155`		`Substrate.`
`BINDING`	`233 233`		`Substrate.`
`MOD_RES`	`224 224`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`113 113`		`S -> H (in Ref. 3).`
`STRAND`	`6 12`	`7`
`HELIX`	`16 26`	`11`
`TURN`	`27 29`	`3`
`STRAND`	`32 37`	`6`
`HELIX`	`41 54`	`14`
`HELIX`	`55 57`	`3`
`STRAND`	`62 64`	`3`
`HELIX`	`69 71`	`3`
`STRAND`	`76 80`	`5`
`HELIX`	`96 112`	`17`
`STRAND`	`117 121`	`5`
`HELIX`	`126 137`	`12`
`STRAND`	`143 146`	`4`
`HELIX`	`148 150`	`3`
`HELIX`	`152 163`	`12`
`HELIX`	`168 170`	`3`
`STRAND`	`175 177`	`3`
`TURN`	`179 182`	`4`
`HELIX`	`212 220`	`9`
`HELIX`	`223 230`	`8`
`HELIX`	`235 249`	`15`
`STRAND`	`254 261`	`8`
`STRAND`	`263 267`	`5`
`STRAND`	`272 280`	`9`
`STRAND`	`283 287`	`5`
`TURN`	`296 299`	`4`
`HELIX`	`300 308`	`9`
`HELIX`	`310 313`	`4`

Sequence information

Length: 317 AA [This is the length of the unprocessed precursor]

Molecular weight: 34863 Da [This is the MW of the unprocessed precursor]

CRC64: 4B146CF681C91046 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKNNGGARVV VIGAGFVGAS YVFALMNQGI ADEIVLIDAN ESKAIGDAMD FNHGKVFAPK 

        70         80         90        100        110        120 
PVDIWHGDYD DCRDADLVVI CAGANQKPGE TRLDLVDKNI AIFRSIVESV MASGFQGLFL 

       130        140        150        160        170        180 
VATNPVDILT YATWKFSGLP HERVIGSGTI LDTARFRFLL GEYFSVAPQN VHAYIIGEHG 

       190        200        210        220        230        240 
DTELPVWSQA YIGVMPIRKL VESKGEEAQK DLERIFVNVR DAAYQIIEKK GATYYGIAMG 

       250        260        270        280        290        300 
LARVTRAILH NENAILTVSA YLDGLYGERD VYIGVPAVIN RNGIREVIEI ELNDDEKNRF 

       310 
HHSAATLKSV LARAFTR

P00344 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