Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1n8ia_ Alpha and beta proteins (a/b) TIM beta/alpha-barrel Malate synthase G Malate synthase G Malate synthase G (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyMalate synthase G 8042001 3000549 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AMalate_synthasee1n8iA1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: Malate_synthaseECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.20.20.360 Alpha Beta Alpha-Beta Barrel TIM Barrel Malate synthase, domain 3CATH (4.3.0)
A2.170.170.11 Mainly Beta Beta Complex Malate synthase G - maily-beta sub-domain Malate synthase G - maily-beta sub-domainCATH (4.3.0)
A1.20.1220.12 Mainly Alpha Up-down Bundle Malate Synthase G Chain: ACATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF20658Malate synthase G, alpha-beta insertion domain (MSG_insertion)Malate synthase G, alpha-beta insertion domainMalate synthase (MS) 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. There have been i ...Malate synthase (MS) 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. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted alpha/beta domain in MSG that may have regulatory function [1,2,3,4]. Members of the isoform G family are only found in bacteria. This entry represents the alpha/beta insertion domain from MSG, which buttressed one side of the TIM-barrel domain [1].
Domain
PF01274Malate synthase, TIM barrel domain (MS_TIM-barrel)Malate synthase, TIM barrel domainMalate synthase (MS) 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. There have been i ...Malate synthase (MS) 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. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted alpha/beta domain in MSG that may have regulatory function [1,2]. In malate synthases, the TIM beta/alpha-barrel fold and the C-terminal domain are well conserved and the cleft between them forms the active site [1,2,3,4]. MSA and MSG consist of an N-terminal alpha-helical clasp domain, a central TIM barrel domain and a C-terminal helical plug domain. This is the TIM barrel domain of malate synthases.
Domain
PF20659Malate synthase, C-terminal (MS_C)Malate synthase, C-terminalMalate synthase (MS) 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. There have been i ...Malate synthase (MS) 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. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted alpha/beta domain in MSG that may have regulatory function [1,2]. In malate synthases, the TIM beta/alpha-barrel fold and the C-terminal helical domain are well conserved and the cleft between them forms the active site [1,2,3,4]. This entry represents the C-terminal domain which consists of a five-helix 'plug' connected to the barrel by an extended loop and caps the active site.
Domain
PF20656Malate synthase, N-terminal domain (MS_N)Malate synthase, N-terminal domainMalate synthase (MS) 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. There have been i ...Malate synthase (MS) 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. There have been identified two isoforms, A and G (MSA and MSG, respectively) that differ in size and is attributed to an inserted alpha/beta domain in MSG that may have regulatory function [1,2]. They consist of an N-terminal alpha-helical claps, a central TIM barrel and a C-terminal alpha-helical plug. This entry represents the N-terminal clasp that wraps around one side of the TIM barrel and buttressed it [1,2,3,4].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Probable malate synthase G

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
malate synthase  M-CSA #53

The discovery of malate synthase proved to be the missing link in closing the tricarboxylic acid cycle, also known as the glyoxylate cycle. Together with isocitrate lyase, malate synthase allows the utilisation of two carbon compounds that would otherwise be wasted. Firstly isocitrate lyase catalyses the cleavage of isocitrate to succinate and glyoxylate (the citric acid cycle would otherwise convert isocitrate to succinate and two molecules of carbon dioxide). Malate synthase then catalyses the Claisen condensation of glyoxylate with an acetyl group from acetyl-CoA to form a malyl-CoA intermediate. This is subsequently hydrolysed, producing malate to replenish the pool of citric-acid-cycle intermediates.

Defined by 4 residues: ARG:A-339GLU:A-434ASP:A-462ASP:A-633
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