A0A6G6W824 · A0A6G6W824_9ACTN
- ProteinMalate synthase G
- GeneglcB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids713 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Catalytic activity
- glyoxylate + acetyl-CoA + H2O = (S)-malate + CoA + H+
Cofactor
Pathway
Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 119 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 126-127 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 269 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 306 | acetyl-CoA (UniProtKB | ChEBI) | |||
Active site | 332 | Proton acceptor | |||
Binding site | 332 | glyoxylate (UniProtKB | ChEBI) | |||
Binding site | 423 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 423 | glyoxylate (UniProtKB | ChEBI) | |||
Binding site | 448-451 | glyoxylate (UniProtKB | ChEBI) | |||
Binding site | 451 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 532 | acetyl-CoA (UniProtKB | ChEBI) | |||
Active site | 623 | Proton donor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | magnesium ion binding | |
Molecular Function | malate synthase activity | |
Biological Process | glyoxylate catabolic process | |
Biological Process | glyoxylate cycle | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMalate synthase G
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Nocardioidaceae > Nocardioides
Accessions
- Primary accessionA0A6G6W824
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 609 | Cysteine sulfenic acid (-SOH) | |||
Keywords
- PTM
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 18-78 | Malate synthase N-terminal | |||
Domain | 161-228 | Malate synthase G alpha-beta insertion | |||
Domain | 329-570 | Malate synthase TIM barrel | |||
Domain | 585-664 | Malate synthase C-terminal | |||
Sequence similarities
Belongs to the malate synthase family. GlcB subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length713
- Mass (Da)77,403
- Last updated2020-08-12 v1
- Checksum0A918FE297C0A202
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP049257 EMBL· GenBank· DDBJ | QIG41374.1 EMBL· GenBank· DDBJ | Genomic DNA |