ID A0A1M6Z9W6_9FLAO Unreviewed; 397 AA. AC A0A1M6Z9W6; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 27-NOV-2024, entry version 30. DE RecName: Full=2-amino-3-ketobutyrate coenzyme A ligase {ECO:0000256|HAMAP-Rule:MF_00985}; DE Short=AKB ligase {ECO:0000256|HAMAP-Rule:MF_00985}; DE EC=2.3.1.29 {ECO:0000256|HAMAP-Rule:MF_00985}; DE AltName: Full=Glycine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_00985}; GN Name=kbl {ECO:0000256|HAMAP-Rule:MF_00985}; GN ORFNames=SAMN05444366_0179 {ECO:0000313|EMBL:SHL27242.1}; OS Flavobacterium saccharophilum. OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=29534 {ECO:0000313|EMBL:SHL27242.1, ECO:0000313|Proteomes:UP000184121}; RN [1] {ECO:0000313|EMBL:SHL27242.1, ECO:0000313|Proteomes:UP000184121} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 1811 {ECO:0000313|EMBL:SHL27242.1, RC ECO:0000313|Proteomes:UP000184121}; RA Jaros S., Januszkiewicz K., Wedrychowicz H.; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine CC and acetyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00985}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glycine + acetyl-CoA = (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 Evidence={ECO:0000256|HAMAP-Rule:MF_00985}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00985}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00985}; CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo- CC reductase pathway; glycine from L-threonine: step 2/2. CC {ECO:0000256|HAMAP-Rule:MF_00985}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00985}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|HAMAP-Rule:MF_00985}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00985}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FRBY01000001; SHL27242.1; -; Genomic_DNA. DR RefSeq; WP_072969785.1; NZ_FRBY01000001.1. DR AlphaFoldDB; A0A1M6Z9W6; -. DR STRING; 29534.SAMN05444366_0179; -. DR OrthoDB; 9807157at2; -. DR UniPathway; UPA00046; UER00506. DR Proteomes; UP000184121; Unassembled WGS sequence. DR GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniRule. DR CDD; cd06454; KBL_like; 1. DR FunFam; 3.90.1150.10:FF:000004; 2-amino-3-ketobutyrate coenzyme A ligase; 1. DR FunFam; 3.40.640.10:FF:000006; 5-aminolevulinate synthase, mitochondrial; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_00985; 2am3keto_CoA_ligase; 1. DR InterPro; IPR011282; 2am3keto_CoA_ligase. DR InterPro; IPR004839; Aminotransferase_I/II_large. DR InterPro; IPR050087; AON_synthase_class-II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR01822; 2am3keto_CoA; 1. DR PANTHER; PTHR13693:SF103; 2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE; 1. DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_00985}; Ligase {ECO:0000313|EMBL:SHL27242.1}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00985}. FT DOMAIN 43..386 FT /note="Aminotransferase class I/classII large" FT /evidence="ECO:0000259|Pfam:PF00155" FT BINDING 136 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985" 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 /evidence="ECO:0000256|HAMAP-Rule:MF_00985" 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 /evidence="ECO:0000256|HAMAP-Rule:MF_00985" FT BINDING 274..275 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985" FT BINDING 368 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985" FT MOD_RES 244 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985" SQ SEQUENCE 397 AA; 43461 MW; F8CB79B910F109B6 CRC64; MYGKIKEHLQ NELQTIEESG IFKKERIITS EQGAEITIST GETVLNFCAN NYLGLSSHPE VVQAAKDTMD THGFGMSSVR FICGTQDIHK TLEKKIADFY GTEDTILYAA AFDANGGVFE PLLGENDAII SDSLNHASII DGVRLCKAAR YRYENSNMED LEQQLIKANE AGARFKLIVT DGVFSMDGLV APLDKICDLA DKYDAMVMVD ECHAAGFIGA TGKGTLEAKG VMGRVDIITG TLGKALGGAM GGYTTAKKEI IELLRQRSRP YLFSNSLAPA IVGASIKVFE LLEKDTSLRD KLEWNTNYFK QGMKEAGFDI IDGDSAIVPV MLYDAKLSQT MANELLNEGI YVIGFFFPVV PKEKARIRVQ LSAAHSKEHL DKAISAFKVV GQKLKVI //