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InterPro: IPR001236 Lactate/malate dehydrogenase

Protein matches Help

UniProtKB

Matches:

5121 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

IPR001236 Lactate/malate_DH

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00056	Ldh_1_N	4967
Pfam	PF02866	Ldh_1_C	4938
Signatures in BioMart

InterPro Relationships Help

Children

IPR001557 L-lactate/malate dehydrogenase
IPR010097 Malate dehydrogenase, NAD-dependent, eukaryote/gamma proteobacteria
IPR010945 Malate dehydrogenase, NAD/NADP

Contains

IPR001252 Malate dehydrogenase, active site
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:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

L-lactate dehydrogenases are metabolic enzymes which catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis [1]. L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyse the interconversion of malate to oxaloacetate [2]. The enzyme participates in the citric acid cycle.

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

Enzyme: EC:1.1.1

PANDIT: PF00056 , PF02866

Pfam Clan: CL0063.21

AC	CL0063.21
ID	NADP_Rossmann
DE	FAD/NAD(P)-binding Rossmann fold Superfamily
PF00044	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
PF00056	IPR001236	Lactate/malate dehydrogenase
PF00070	IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00106	IPR002198	Short-chain dehydrogenase/reductase SDR
PF00107	IPR013149	Alcohol dehydrogenase, zinc-binding
PF00208	IPR006096	Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
PF00479	IPR001282	Glucose-6-phosphate dehydrogenase
PF00670	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding
PF00732	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
PF00743	IPR000960	Flavin-containing monooxygenase FMO
PF00890	IPR003953	Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00899	IPR000594	UBA/THIF-type NAD/FAD binding fold
PF00996	IPR018203	GDP dissociation inhibitor
PF01073	IPR002225	3-beta hydroxysteroid dehydrogenase/isomerase
PF01113	IPR000846	Dihydrodipicolinate reductase
PF01118	IPR000534	Semialdehyde dehydrogenase, NAD-binding
PF01134	IPR002218	Glucose-inhibited division protein A-related
PF01210	IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01225	IPR000713	Mur ligase, N-terminal
PF01232	IPR013131	Mannitol dehydrogenase, N-terminal
PF01262	IPR007698	Alanine dehydrogenase/PNT, C-terminal
PF01266	IPR006076	FAD dependent oxidoreductase
PF01370	IPR001509	NAD-dependent epimerase/dehydratase
PF01408	IPR000683	Oxidoreductase, N-terminal
PF01488	IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
PF01494	IPR002938	Monooxygenase, FAD-binding
PF01593	IPR002937	Amine oxidase
PF01946	IPR002922	Thiamine biosynthesis Thi4 protein
PF02153	IPR003099	Prephenate dehydrogenase
PF02254	IPR003148	Regulator of K+ conductance, N-terminal
PF02423	IPR003462	Ornithine cyclodeaminase/mu-crystallin
PF02558	IPR013332	Ketopantoate reductase ApbA/PanE, N-terminal
PF02629	IPR003781	CoA-binding
PF02670	IPR013512	1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02719	IPR003869	Polysaccharide biosynthesis protein CapD-like
PF02737	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
PF02826	IPR006140	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02882	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
PF03435	IPR005097	Saccharopine dehydrogenase
PF03446	IPR006115	6-phosphogluconate dehydrogenase, NAD-binding
PF03447	IPR005106	Aspartate/homoserine dehydrogenase, NAD-binding
PF03486	IPR004792	HI0933-like protein
PF03721	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03807	IPR004455	NADP oxidoreductase, coenzyme F420-dependent
PF03949	IPR012302	Malic enzyme, NAD-binding
PF04321	IPR005913	dTDP-4-dehydrorhamnose reductase
PF04723	IPR006812	Glycine reductase complex selenoprotein A
PF04820	IPR006905	Tryptophan halogenase
PF05368	IPR008030	NmrA-like
PF05834	IPR008671	Lycopene beta/epsilon cyclase
PF06039	IPR006231	Malate:quinone-oxidoreductase
PF07157	IPR009826	DNA circulation, N-terminal
PF07991	IPR013116	Acetohydroxy acid isomeroreductase, catalytic
PF07992	IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PF07993	IPR013120	Male sterility, NAD-binding
PF07994	IPR002587	Myo-inositol-1-phosphate synthase
PF08491	IPR013698	Squalene epoxidase
PF08659	IPR013968	Polyketide synthase, KR
PF10727	IPR019665	Putative oxidoreductase/dehydrogenase, Rossmann-like domain

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001236

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O02640 Probable malate dehydrogenase, mitochondrial

P00338 L-lactate dehydrogenase A chain

P00342 L-lactate dehydrogenase C chain

P17505 Malate dehydrogenase, mitochondrial

Q95028 L-lactate dehydrogenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001236	Lactate/malate dehydrogenase
IPR001252	Malate dehydrogenase, active site
IPR011304	L-lactate dehydrogenase
IPR001557	L-lactate/malate dehydrogenase
IPR015955	Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
IPR016040	NAD(P)-binding domain
IPR010097	Malate dehydrogenase, NAD-dependent, eukaryote/gamma proteobacteria
IPR018177	L-lactate dehydrogenase, active site
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	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 43 175-85 2001 [PubMed: 11276087] http://dx.doi.org/10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#
2.	Gleason WB, Fu Z, Birktoft J, Banaszak L. Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases. Biochemistry 33 2078-88 1994 [PubMed: 8117664] http://dx.doi.org/10.1021/bi00174a014

Additional Reading Open in usermanual
	Kawakami R, Sakuraba H, Goda S, Tsuge H, Ohshima T. Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix. Biochim. Biophys. Acta 1794 2009 1496-504 [PubMed: 19555779]
	Fioravanti E, Vellieux FM, Amara P, Madern D, Weik M. Specific radiation damage to acidic residues and its relation to their chemical and structural environment. 14 2007 84-91 [PubMed: 17211074] http://dx.doi.org/10.1107/S0909049506038623
	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
	Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R. Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol. Biochem. Parasitol. 151 2007 100-10 [PubMed: 17125854] http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
	Chapman AD, Cortes A, Dafforn TR, Clarke AR, Brady RL. Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD. J. Mol. Biol. 285 1999 703-12 [PubMed: 10075524] http://dx.doi.org/10.1006/jmbi.1998.2357
	Cox B, Chit MM, Weaver T, Gietl C, Bailey J, Bell E, Banaszak L. Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence. FEBS J. 272 2005 643-54 [PubMed: 15670147] http://dx.doi.org/10.1111/j.1742-4658.2004.04475.x
	Madern D. Molecular evolution within the L-malate and L-lactate dehydrogenase super-family. J. Mol. Evol. 54 2002 825-40 [PubMed: 12029364] http://dx.doi.org/10.1007/s00239-001-0088-8

InterPro 23.1