Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyGABA-aminotransferase-like 8020637 4000675 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyPLP-dependent transferases 8033017 3000954 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyPLP-dependent transferases 8033017 3000954 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AAminotran_1_2_C_9e1fc4A1 A: a+b two layersX: C-terminal domain in some PLP-dependent transferases (From Topology)H: C-terminal domain in some PLP-dependent transferases (From Topology)T: C-terminal domain in some PLP-dependent transferasesF: Aminotran_1_2_C_9ECOD (1.6)
AAminotran_5_Ne1fc4A2 A: a/b three-layered sandwichesX: PLP-dependent transferases (From Topology)H: PLP-dependent transferases (From Topology)T: PLP-dependent transferasesF: Aminotran_5_NECOD (1.6)
BAminotran_1_2_C_9e1fc4B3 A: a+b two layersX: C-terminal domain in some PLP-dependent transferases (From Topology)H: C-terminal domain in some PLP-dependent transferases (From Topology)T: C-terminal domain in some PLP-dependent transferasesF: Aminotran_1_2_C_9ECOD (1.6)
BAminotran_5_Ne1fc4B2 A: a/b three-layered sandwichesX: PLP-dependent transferases (From Topology)H: PLP-dependent transferases (From Topology)T: PLP-dependent transferasesF: Aminotran_5_NECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00155Aminotransferase class I and II (Aminotran_1_2)Aminotransferase class I and II- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
2-AMINO-3-KETOBUTYRATE CONENZYME A LIGASE

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

ChainsEnzyme NameDescriptionCatalytic Residues
glycine C-acetyltransferase  M-CSA #762

Threonine is degraded into glycine and the acetyl group in a pathway common to prokaryotic and eukaryotic cells. The pathway is two steps long; the first step is the oxidation of the hydroxy group of threonine to create 2-amino-3-ketobutyrate by L-threonine dehydrogenase. The second step is catalysed by 2-amino-3-ketobutyrate CoA ligase (KBL); this is a PLP-dependent acetyltransferase, transferring the newly formed acetyl group of the substrate to Coenzyme A to give glycine and acetyl-CoA. The two enzymes needed for the pathway form a complex; this is because the aminoketobutyrate intermediate (substrate for KBL) spontaneously decarboxylates in aqueous solution.

Defined by 3 residues: SER:A-188 [auth A-185]HIS:A-216 [auth A-213]LYS:A-247 [auth A-244]
 | 
 
Explore in 3DM-CSA Motif Definition