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InterPro: IPR001465 Malate synthase

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UniProtKB

Matches:

1153 proteins

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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

IPR001465 Malate_synthase

Type

Family

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR21631:SF1	Malate_synthase	1153
Signatures in BioMart

InterPro Relationships Help

Children

IPR006252 Malate synthase A
IPR006253 Malate synthase G

Contains

IPR011076 Malate synthase-like, core
IPR019830 Malate synthase, conserved site

GO Term annotation Help

Process

GO:0006097 glyoxylate cycle

Function

GO:0004474 malate synthase activity

InterPro annotation

Entry Details in BioMart

Abstract

Malate synthase (EC:2.3.3.9) catalyses the aldol condensation of glyoxylate with acetyl-CoA to form malate as part of the second step of the glyoxylate bypass and an alternative to the tricarboxylic acid cycle in bacteria, fungi and plants. Malate synthase has a TIM beta/alpha-barrel fold [1].

Structural links Help

PDB - click here

SCOP: c.1.13.1

CATH: 1.20.1220.12 , 2.170.170.11 , 3.20.20.360

Database links Help

PDBe-motif: PS00510

Enzyme: EC:2.3.3.9

PROSITE doc: PDOC00441

PANDIT: PF01274

Blocks: IPB001465

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001465

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A6ZRW6 Malate synthase 1, glyoxysomal

P08216 Malate synthase, glyoxysomal

P08997 Malate synthase A

P21360 Malate synthase, glyoxysomal

Q8T2K9 Malate synthase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR019830	Malate synthase, conserved site
IPR011076	Malate synthase-like, core
IPR001465	Malate synthase
IPR006252	Malate synthase A
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Howard BR, Endrizzi JA, Remington SJ. Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications. Biochemistry 39 3156-68 2000 [PubMed: 10715138] http://dx.doi.org/10.1021/bi992519h

Additional Reading Open in usermanual
	Anstrom DM, Kallio K, Remington SJ. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 A resolution. Protein Sci. 12 2003 1822-32 [PubMed: 12930982] http://dx.doi.org/10.1110/ps.03174303
	Anstrom DM, Remington SJ. The product complex of M. tuberculosis malate synthase revisited. Protein Sci. 15 2006 2002-7 [PubMed: 16877713] http://dx.doi.org/10.1110/ps.062300206
	Tugarinov V, Choy WY, Orekhov VY, Kay LE. Solution NMR-derived global fold of a monomeric 82-kDa enzyme. Proc. Natl. Acad. Sci. U.S.A. 102 2005 622-7 [PubMed: 15637152] http://dx.doi.org/10.1073/pnas.0407792102
	Smith CV, Huang CC, Miczak A, Russell DG, Sacchettini JC, Honer zu Bentrup K. Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 278 2003 1735-43 [PubMed: 12393860] http://dx.doi.org/10.1074/jbc.M209248200
	Grishaev A, Tugarinov V, Kay LE, Trewhella J, Bax A. Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints. J. Biomol. NMR 40 2008 95-106 [PubMed: 18008171] http://dx.doi.org/10.1007/s10858-007-9211-5

InterPro 23.1