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InterPro: IPR006253 Malate synthase G

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UniProtKB

Matches:

349 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR006253 Malate_synthG

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01345	malate_syn_G	349
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001465 Malate synthase

Contains

IPR011076 Malate synthase-like, core

GO Term annotation Help

Process

GO:0006097 glyoxylate cycle

Function

GO:0004474 malate synthase activity

InterPro annotation

Entry Details in BioMart

Abstract

These sequences represent the G isozyme of malate synthase. Malate synthase G (MSG, 723 residues) is an enzyme of the glyoxylate pathway, that catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA [1], this biochemical bypass is used by microorganisms (bacteria, yeast, and fungi) for biosynthesis under anaerobic conditions [2]. Enzymes of the glyoxylate bypass have been implicated as virulence factors in several pathogens, including Mycobacterium tuberculosis [3, 4, 5].

The X-ray structure of the ternary abortive complex of MSG with pyruvate (glyoxylate mimic) and acetyl-CoA has been determined [1] and shown to have the same structure as in the complex with glyoxylate [6].

Structural links Help

PDB - click here

SCOP: c.1.13.1

CATH: 1.10.1860.10 , 1.20.1220.12 , 2.170.170.11 , 3.20.20.360

Database links Help

Enzyme: EC:2.3.3.9

CluSTr: ALLvsALL:33882:43.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006253

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0A5J4 Malate synthase G

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011076	Malate synthase-like, core
IPR006253	Malate synthase G
IPR001465	Malate synthase
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	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 1822-32 2003 [PubMed: 12930982] http://dx.doi.org/10.1110/ps.03174303
2.	KORNBERG HL, KREBS HA. Synthesis of cell constituents from C2-units by a modified tricarboxylic acid cycle. Nature 179 988-91 1957 [PubMed: 13430766]
3.	Bishai W. Lipid lunch for persistent pathogen. Nature 406 683-5 2000 [PubMed: 10963578] http://dx.doi.org/10.1038/35021159
4.	McKinney JD, Honer zu Bentrup K, Munoz-Elias EJ, Miczak A, Chen B, Chan WT, Swenson D, Sacchettini JC, Jacobs WR Jr, Russell DG. Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature 406 735-8 2000 [PubMed: 10963599] http://dx.doi.org/10.1038/35021074
5.	Lorenz MC, Fink GR. The glyoxylate cycle is required for fungal virulence. Nature 412 83-6 2001 [PubMed: 11452311] http://dx.doi.org/10.1038/35083594
6.	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, 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