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InterPro: IPR011304 L-lactate dehydrogenase

Protein matches Help

UniProtKB

Matches:

1308 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR011304 L-lactate_DH

Secondary

IPR001557 , IPR010947

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01771	L-LDH-NAD	1308
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001557 L-lactate/malate dehydrogenase

Contains

IPR015955 Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
IPR016040 NAD(P)-binding domain
IPR018177 L-lactate dehydrogenase, active site

GO Term annotation Help

Process

GO:0019642 anaerobic glycolysis
GO:0055114 oxidation reduction

Function

GO:0004459 L-lactate dehydrogenase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents the NAD-dependent L-lactate dehydrogenases from bacteria and eukaryotes. This enzyme functions as the final step in anaerobic glycolysis. Although lactate dehydrogenases have in some cases been mistaken for malate dehydrogenases due to the similarity of these two substrates and the apparent ease with which evolution can toggle these activities, critical residues have been identified [1] which can discriminate between the two activities.

Structural links Help

PDB - click here

SCOP: c.2.1.5 , d.162.1.1 , i.12.1.1

CATH: 3.40.50.720 , 3.90.110.10

Database links Help

PDBe-motif: PS00064

Enzyme: EC:1.1.1.27

PROSITE doc: PDOC00062

CluSTr: ALLvsALL:2334:60.8

PRIAM: PRI000821

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011304

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00338 L-lactate dehydrogenase A chain

P00342 L-lactate dehydrogenase C chain

P00343 L-lactate dehydrogenase

Q27888 L-lactate dehydrogenase

Q95028 L-lactate dehydrogenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001236	Lactate/malate dehydrogenase
IPR016040	NAD(P)-binding domain
IPR011304	L-lactate dehydrogenase
IPR018177	L-lactate dehydrogenase, active site
IPR001557	L-lactate/malate dehydrogenase
IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Hannenhalli SS, Russell RB. Analysis and prediction of functional sub-types from protein sequence alignments. J. Mol. Biol. 303 61-76 2000 [PubMed: 11021970] http://dx.doi.org/10.1006/jmbi.2000.4036

Additional Reading Open in usermanual
	Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins 43 2001 175-85 [PubMed: 11276087] http://dx.doi.org/10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#
	Uchikoba H, Fushinobu S, Wakagi T, Konno M, Taguchi H, Matsuzawa H. Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces. Proteins 46 2002 206-14 [PubMed: 11807949] http://dx.doi.org/10.1002/prot.1165
	Coquelle N, Fioravanti E, Weik M, Vellieux F, Madern D. Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments. J. Mol. Biol. 374 2007 547-62 [PubMed: 17936781] http://dx.doi.org/10.1016/j.jmb.2007.09.049
	Auerbach G, Ostendorp R, Prade L, Korndorfer I, Dams T, Huber R, Jaenicke R. Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization. Structure 6 1998 769-81 [PubMed: 9655830] http://dx.doi.org/10.1016/S0969-2126(98)00078-1
	Cameron A, Read J, Tranter R, Winter VJ, Sessions RB, Brady RL, Vivas L, Easton A, Kendrick H, Croft SL, Barros D, Lavandera JL, Martin JJ, Risco F, Garcia-Ochoa S, Gamo FJ, Sanz L, Leon L, Ruiz JR, Gabarro R, Mallo A, Gomez de las Heras F. Identification and activity of a series of azole-based compounds with lactate dehydrogenase-directed anti-malarial activity. J. Biol. Chem. 279 2004 31429-39 [PubMed: 15117937] http://dx.doi.org/10.1074/jbc.M402433200

InterPro 24.0