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InterPro: IPR003767 Malate/L-lactate dehydrogenase

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949 proteins

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Accession

IPR003767 Malate/L-lactate_DH

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02615	Ldh_2	927
PANTHER	PTHR11091	MDH_LDH	920
SuperFamily	SSF89733	MDH_LDH	943
Signatures in BioMart

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Children

IPR017590 Ureidoglycolate dehydrogenase

GO Term annotation Help

Process

GO:0008152 metabolic process
GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

The malate dehydrogenase (MDH) of some extremophilies is more similar to the L-lactate dehydrogenases (L-LDH) EC:1.1.1.27 from various sources than to other MDHs [1].

This family consists of bacterial and archaeal malate/L-lactate dehydrogenases. The archaebacterial malate dehydrogenase EC:1.1.1.37, EC:1.1.1.82 deviates from the eubacterial and eukaryotic enzymes having a low selectivity for the coenzyme (NAD(H) or NADP(H)) and catalyzing the reduction of oxalacetate to malate more efficiently than the reverse reaction [2].

Structural links Help

PDB - click here

SCOP: c.122.1.1

CATH: 1.10.1530.10 , 3.30.1370.60 , 3.30.60.50

Database links Help

Enzyme: EC:1.1.1

PANDIT: PF02615

Blocks: IPB003767

CluSTr: ALLvsALL:35681:43.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003767

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O59028 Malate dehydrogenase

P30178 Uncharacterized oxidoreductase ybiC

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003767	Malate/L-lactate dehydrogenase
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Cendrin F, Chroboczek J, Zaccai G, Eisenberg H, Mevarech M. Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry 32 4308-13 1993 [PubMed: 8476859] http://dx.doi.org/10.1021/bi00067a020
2.	Honka E, Fabry S, Niermann T, Palm P, Hensel R. Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus. Eur. J. Biochem. 188 623-32 1990 [PubMed: 2110059] http://dx.doi.org/10.1111/j.1432-1033.1990.tb15443.x

Additional Reading Open in usermanual
	Forouhar F, Lee I, Benach J, Kulkarni K, Xiao R, Acton TB, Montelione GT, Tong L. A novel NAD-binding protein revealed by the crystal structure of 2,3-diketo-L-gulonate reductase (YiaK). J. Biol. Chem. 279 2004 13148-55 [PubMed: 14718529] http://dx.doi.org/10.1074/jbc.M313580200
	Irimia A, Madern D, Zaccai G, Vellieux FM. Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes. EMBO J. 23 2004 1234-44 [PubMed: 15014443] http://dx.doi.org/10.1038/sj.emboj.7600147
	Jendrossek D, Kratzin HD, Steinbuchel A. The Alcaligenes eutrophus ldh structural gene encodes a novel type of lactate dehydrogenase. FEMS Microbiol. Lett. 112 1993 229-35 [PubMed: 8405966] http://dx.doi.org/10.1016/0378-1097(93)90169-3

InterPro 23.1