Function and Biology Details
Reaction catalysed:
[Protein]-S(8)-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glycine cleavage system H-protein/Simiate
- Glycine cleavage system H-protein
- Glycine cleavage T-protein, C-terminal barrel domain
- Glycine cleavage T-protein/YgfZ, C-terminal
- Aminomethyltransferase, folate-binding domain
- GTP-binding protein TrmE/Aminomethyltransferase GcvT, domain 1
- Aminomethyltransferase-like
- Glycine cleavage system T protein
5 more domains
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-141427 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aminomethyltransferase
Molecule details ›
Chains: A, B, C, D
Length: 364 amino acids
Theoretical weight: 40.19 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 364 amino acids
Theoretical weight: 40.19 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P27248 (Residues: 1-364; Coverage: 100%)
Sequence domains:
Structure domains:
Glycine cleavage system H protein
Molecule details ›
Chains: E, F
Length: 129 amino acids
Theoretical weight: 14.01 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Glycine cleavage H-protein
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 129 amino acids
Theoretical weight: 14.01 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P0A6T9 (Residues: 1-129; Coverage: 100%)
Sequence domains: Glycine cleavage H-protein
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
