[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 393 / DSM 20011 / IFO 15883 / JCM 1134 / NCDO 161; PubMed=1768113 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.F., Baek S.J., Pack M.Y.; "Cloning and nucleotide sequence of the Lactobacillus casei lactate dehydrogenase gene."; Appl. Environ. Microbiol. 57:2413-2417(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 393 / DSM 20011 / IFO 15883 / JCM 1134 / NCDO 161; Taguchi H., Ohta T.; Submitted (NOV-1991) to the PIR data bank.
[3]	PROTEIN SEQUENCE OF 2-326. PubMed=6411465 [NCBI, ExPASy, EBI, Israel, Japan] Hensel R., Mayr U., Yang C.; "The complete primary structure of the allosteric L-lactate dehydrogenase from Lactobacillus casei."; Eur. J. Biochem. 134:503-511(1983).
[4]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). Buehner M., Hecht H.J.; "Structure determination of the allosteric L-lactate dehydrogenase from Lactobacillus-casei at 3A resolution."; Acta Crystallogr. A 40:32-34(1984).

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

D12591; BAA02133.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M76708; AAA25245.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A43944; DELBLA.

3D structure databases

PDB

1LLC; X-ray; 3.00 A; A=2-326.

[ExPASy / RCSB / EBI]

PDBsum

1LLC; -.

ModBase

P00343.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-8681; -.

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

P00343; -.

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`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 326`	`325`	`L-lactate dehydrogenase.`	`PRO_0000168347`
`NP_BIND`	`18 46`	`29`	`NAD (By similarity).`
`ACT_SITE`	`181 181`		`Proton acceptor (By similarity).`
`BINDING`	`94 94`		`Substrate (By similarity).`
`BINDING`	`126 126`		`NAD or substrate (By similarity).`
`BINDING`	`157 157`		`Substrate (By similarity).`
`BINDING`	`235 235`		`Substrate (By similarity).`
`MOD_RES`	`226 226`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`26 26`		`Y -> F (in Ref. 3; AA sequence).`
`CONFLICT`	`52 52`		`I -> T (in Ref. 3; AA sequence).`
`CONFLICT`	`88 89`		`QK -> KQ (in Ref. 3; AA sequence).`
`CONFLICT`	`119 119`		`G -> L (in Ref. 3; AA sequence).`
`CONFLICT`	`270 270`		`L -> I (in Ref. 3; AA sequence).`
`CONFLICT`	`273 273`		`I -> L (in Ref. 3; AA sequence).`
`STRAND`	`12 14`	`3`
`TURN`	`17 18`	`2`
`HELIX`	`19 31`	`13`
`TURN`	`32 32`	`1`
`STRAND`	`37 39`	`3`
`HELIX`	`45 54`	`10`
`TURN`	`55 56`	`2`
`TURN`	`59 60`	`2`
`TURN`	`70 74`	`5`
`STRAND`	`79 81`	`3`
`TURN`	`84 84`	`1`
`TURN`	`96 96`	`1`
`HELIX`	`97 100`	`4`
`TURN`	`101 102`	`2`
`TURN`	`104 109`	`6`
`HELIX`	`110 114`	`5`
`TURN`	`115 116`	`2`
`STRAND`	`120 122`	`3`
`HELIX`	`128 139`	`12`
`TURN`	`143 145`	`3`
`TURN`	`150 151`	`2`
`HELIX`	`152 165`	`14`
`TURN`	`170 171`	`2`
`STRAND`	`174 179`	`6`
`STRAND`	`186 193`	`8`
`TURN`	`195 196`	`2`
`TURN`	`216 221`	`6`
`HELIX`	`222 224`	`3`
`TURN`	`225 228`	`4`
`TURN`	`235 236`	`2`
`HELIX`	`237 252`	`16`
`TURN`	`253 253`	`1`
`STRAND`	`278 282`	`5`
`TURN`	`283 284`	`2`
`STRAND`	`285 289`	`5`
`TURN`	`295 296`	`2`
`HELIX`	`297 303`	`7`
`TURN`	`304 316`	`13`

Sequence information

Length: 326 AA [This is the length of the unprocessed precursor]

Molecular weight: 35531 Da [This is the MW of the unprocessed precursor]

CRC64: 934905641592AF8A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASITDKDHQ KVILVGDGAV GSSYAYAMVL QGIAQEIGIV DIFKDKTKGD AIDLSNALPF 

        70         80         90        100        110        120 
TSPKKIYSAE YSDAKDADLV VITAGAPQKP GETRLDLVNK NLKILKSIVD PIVDSGFNGI 

       130        140        150        160        170        180 
FLVAANPVDI LTYATWKLSG FPKNRVVGSG TSLDTARFRQ SIAEMVNVDA RSVHAYIMGE 

       190        200        210        220        230        240 
HGDTEFPVWS HANIGGVTIA EWVKAHPEIK EDKLVKMFED VRDAAYEIIK LKGATFYGIA 

       250        260        270        280        290        300 
TALARISKAI LNDENAVLPL SVYMDGQYGL NDIYIGTPAV INRNGIQNIL EIPLTDHEEE 

       310        320 
SMQKSASQLK KVLTDAFAKN DIETRQ

P00343 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