ID A0A1M6Z9W6_9FLAO Unreviewed; 397 AA. AC A0A1M6Z9W6; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 20-DEC-2017, entry version 8. 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; Bacteroidetes; 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 CC glycine and acetyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00985}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + glycine = CoA + 2-amino-3- CC oxobutanoate. {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 CC oxydo-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 CC of 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 GeneID; 33996368; -. 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 Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00985; 2am3keto_CoA_ligase; 1. DR InterPro; IPR011282; 2am3keto_CoA_ligase. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2. DR PANTHER; PTHR13693:SF60; PTHR13693:SF60; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01822; 2am3keto_CoA; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00985}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000184121}; KW 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 Aminotran_1_2. {ECO:0000259|Pfam: FT PF00155}. FT REGION 241 244 Pyridoxal phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_00985}. FT REGION 274 275 Pyridoxal phosphate binding; shared with FT dimeric partner. {ECO:0000256|HAMAP-Rule: FT MF_00985}. FT COILED 151 171 {ECO:0000256|SAM:Coils}. FT BINDING 136 136 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00985}. FT BINDING 185 185 Pyridoxal phosphate. {ECO:0000256|HAMAP- FT Rule:MF_00985}. FT BINDING 368 368 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00985}. FT MOD_RES 244 244 N6-(pyridoxal phosphate)lysine. FT {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 //