ID   A0A1M6Z9W6_9FLAO        Unreviewed;       397 AA.
AC   A0A1M6Z9W6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JUL-2024, entry version 28.
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=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         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}.
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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:0005829; C:cytosol; IEA:TreeGrafter.
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   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.
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|HAMAP-Rule:MF_00985};
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
FT                   /note="Aminotransferase class I/classII"
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
//