ID A0A0S7BZM7_9BACT Unreviewed; 397 AA.
AC A0A0S7BZM7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=TBC1_112184 {ECO:0000313|EMBL:GAP44023.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP44023.1};
RN [1] {ECO:0000313|EMBL:GAP44023.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP44023.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
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; DF968182; GAP44023.1; -; Genomic_DNA.
DR RefSeq; WP_062042115.1; NZ_DF968182.1.
DR AlphaFoldDB; A0A0S7BZM7; -.
DR STRING; 1678841.TBC1_112184; -.
DR PATRIC; fig|1678841.3.peg.2443; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00046; UER00506.
DR Proteomes; UP000053091; 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 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; 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:GAP44023.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985};
KW Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00985}.
FT DOMAIN 43..384
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
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 /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
FT BINDING 183
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 239..242
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 272..273
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 366
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
SQ SEQUENCE 397 AA; 43691 MW; 0A7759CF4775A43B CRC64;
MYDRLQAHLQ KELADIREAG LYKNERVITT PQGAEIKVNS GAEVLNFCAN NYLGLSNNPK
LIAAAKEALD SHGYGLSSVR FICGTQDLHK RLEAKIAEFF GTEDTILYAA CFDANGGVFE
PLLGEEDAII SDSLNHASII DGVRLCKAQR YRYANADMAD LEEQLKLAQA QRFRLIVTDG
VFSMDGNVAP MDKIHELAQK YDAMVMVDEC HSAGVVGETG RGVTELFNIR GKIEIITGTL
GKAFGGAIGG FTTGKKEIIE MLRQRSRPYL FSNSIPPTVA SAGIKMFDMM AETNELQDRL
HENTAYFVKR MVDAGFDIKP TRSAICAVML YDAKLSQDMA AKLLDEGIYV IGFYYPVVPK
GQARIRVQIS AAHKREHLDK CIAAFTKVGK ELGVLKG
//
