[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 2-332. 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]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)IN COMPLEX WITH NAD AND SUBSTRATE ANALOG. PubMed=1678537 [NCBI, ExPASy, EBI, Israel, Japan] Dunn C.R., Wilks H.M., Halsall D.J., Atkinson T., Clarke A.R., Muirhead H., Holbrook J.J.; "Design and synthesis of new enzymes based on the lactate dehydrogenase framework."; Philos. Trans. R. Soc. Lond., B, Biol. Sci. 332:177-184(1991).

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

U07178; AAA50436.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A00348; DEPGLM.

3D structure databases

PDB

9LDB; X-ray; 2.20 A; A/B=1-332.	[ExPASy / RCSB / EBI]
9LDT; X-ray; 2.00 A; A/B=1-332.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

9LDB; -.
9LDT; -.

ModBase

P00339.

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.

Phylogenomic databases

HOVERGEN

P00339; -.

Other

LinkHub

P00339; -.

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`	`2 332`	`331`	`L-lactate dehydrogenase A chain.`	`PRO_0000168416`
`NP_BIND`	`29 57`	`29`	`NAD.`
`ACT_SITE`	`193 193`		`Proton acceptor.`
`BINDING`	`99 99`		`NAD.`
`BINDING`	`106 106`		`Substrate.`
`BINDING`	`138 138`		`NAD or substrate.`
`BINDING`	`169 169`		`Substrate.`
`BINDING`	`248 248`		`Substrate.`
`MOD_RES`	`2 2`		`N-acetylalanine.`
`MOD_RES`	`239 239`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`233 233`		`Q -> E (in Ref. 2; AA sequence).`
`CONFLICT`	`286 286`		`D -> N (in Ref. 2; AA sequence).`
`HELIX`	`3 7`	`5`
`STRAND`	`8 10`	`3`
`STRAND`	`19 25`	`7`
`HELIX`	`29 40`	`12`
`STRAND`	`45 50`	`6`
`HELIX`	`54 66`	`13`
`HELIX`	`67 70`	`4`
`STRAND`	`75 81`	`7`
`HELIX`	`82 85`	`4`
`STRAND`	`89 93`	`5`
`HELIX`	`105 108`	`4`
`HELIX`	`109 126`	`18`
`STRAND`	`131 134`	`4`
`STRAND`	`136 138`	`3`
`HELIX`	`139 150`	`12`
`STRAND`	`156 159`	`4`
`HELIX`	`163 177`	`15`
`HELIX`	`181 183`	`3`
`STRAND`	`184 190`	`7`
`STRAND`	`192 205`	`14`
`HELIX`	`210 213`	`4`
`STRAND`	`218 221`	`4`
`HELIX`	`227 244`	`18`
`HELIX`	`249 263`	`15`
`STRAND`	`268 275`	`8`
`STRAND`	`279 281`	`3`
`STRAND`	`287 295`	`9`
`STRAND`	`298 303`	`6`
`HELIX`	`311 329`	`19`

Sequence information

Length: 332 AA [This is the length of the unprocessed precursor]

Molecular weight: 36619 Da [This is the MW of the unprocessed precursor]

CRC64: FD3B4673557C9B72 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATLKDQLIH NLLKEEHVPH NKITVVGVGA VGMACAISIL MKELADEIAL VDVMEDKLKG 

        70         80         90        100        110        120 
EMMDLQHGSL FLRTPKIVSG KDYNVTANSR LVVITAGARQ QEGESRLNLV QRNVNIFKFI 

       130        140        150        160        170        180 
IPNIVKYSPN CKLLVVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV 

       190        200        210        220        230        240 
HPLSCHGWIL GEHGDSSVPV WSGVNVAGVS LKNLHPELGT DADKEHWKAV HKQVVDSAYE 

       250        260        270        280        290        300 
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGIKEDVFLS VPCILGQNGI 

       310        320        330 
SDVVKVTLTP EEEAHLKKSA DTLWGIQKEL QF

P00339 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