AC   MF_00985;
DC   Protein; auto
TR   HAMAP; MF_00985; -; 1; level=0
XX
Names: 2am3keto_CoA_ligase
XX
ID   KBL
DE   RecName: Full=2-amino-3-ketobutyrate coenzyme A ligase;
DE            Short=AKB ligase;
DE            EC=2.3.1.29;
DE   AltName: Full=Glycine acetyltransferase;
GN   Name=kbl;
XX
CC   -!- FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine
CC       and acetyl-CoA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA;
CC         Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC       Note=Binds 1 pyridoxal phosphate per subunit.;
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC       reductase pathway; glycine from L-threonine: step 2/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
XX
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1; trigger=no
DR   Pfam; PF00155; Aminotran_1_2; 1; trigger=no
DR   NCBIfam; TIGR01822; 2am3keto_CoA; 1; trigger=no
XX
KW   Acyltransferase
KW   Pyridoxal phosphate
KW   Transferase
XX
GO   GO:0008890; F:glycine C-acetyltransferase activity
GO   GO:0030170; F:pyridoxal phosphate binding
GO   GO:0019518; P:L-threonine catabolic process to glycine
XX
FT   From: KBL_ECOLI (P0AB77)
FT   BINDING         111..112
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Optional; Condition: C-[FY]
FT   BINDING         210..213
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Optional; Condition: [DE]-[DE]-S-H
FT   BINDING         241..244
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Optional; Condition: T-[LF]-G-K
FT   BINDING         274..275
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Optional; Condition: S-N
FT   BINDING         136
FT                   /ligand="substrate"
FT   Optional; Condition: H
FT   BINDING         185
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Optional; Condition: S
FT   BINDING         368
FT                   /ligand="substrate"
FT   Optional; Condition: R
FT   MOD_RES         244
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
XX
Size: 378-460;
Related: None;
Template: P0AB77;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.10 2023/06/01
//