A0A2S8JLX6 · A0A2S8JLX6_ECOLX
- ProteinMalate synthase G
- GeneglcB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids723 (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 | 118 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 125-126 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: RY | ||||||
Binding site | 274 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 311 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 338 | Proton acceptor | ||||
Sequence: R | ||||||
Binding site | 338 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 427 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 427 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 452-455 | glyoxylate (UniProtKB | ChEBI) | ||||
Sequence: GFLD | ||||||
Binding site | 455 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 536 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Active site | 631 | Proton donor | ||||
Sequence: D |
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 > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A2S8JLX6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 617 | Cysteine sulfenic acid (-SOH) | ||||
Sequence: C | ||||||
Modified residue | 688 | Cysteine sulfenic acid (-SOH) | ||||
Sequence: C |
Keywords
- PTM
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-77 | Malate synthase N-terminal | ||||
Sequence: FKRFVDEEVLPGTGLDTAAFWRNFDEIVHDLAPENRQLLAERDRIQAALDEWHRSNPGPVKD | ||||||
Domain | 158-233 | Malate synthase G alpha-beta insertion | ||||
Sequence: YDPQRGEQVIAWVRRFLDESLPLENGSYQDVLAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKN | ||||||
Domain | 335-579 | Malate synthase TIM barrel | ||||
Sequence: LFIRNVGHLMTIPVIWDSEGNEIPEGILDGVMTGAIALYDLKVQKNSRTGSVYIVKPKMHGPQEVAFANKLFTRVETMLGMAPNTLKMGIMDEERRTSLNLRSCIAQARNRVAFINTGFLDRTGDEMHSVMEAGPMLRKNQMKTTPWIKAYERNNVLSGLFCGLRGKAQIGKGMWAMPDLMADMYSQKGDQLRAGANTAWVPSPTAATLHALHYHQTNVQSVQANIAQSEFNAEFEPLLDDLLTI | ||||||
Domain | 591-695 | Malate synthase C-terminal | ||||
Sequence: EIQQELDNNVQGILGYVVRWVEQGIGCSKVPDIHNVALMEDRATLRISSQHIANWLRHGILTKEQVQASLENMAKVVDQQNAGDPAYRPMAGNFANSCAFKAASD |
Sequence similarities
Belongs to the malate synthase family. GlcB subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length723
- Mass (Da)80,567
- Last updated2018-07-18 v1
- ChecksumCA7D3F0789BDC360