ID A0A1H9FYB0_9FLAO Unreviewed; 395 AA.
AC A0A1H9FYB0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05421824_1607 {ECO:0000313|EMBL:SEQ42488.1};
OS Hyunsoonleella jejuensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=419940 {ECO:0000313|EMBL:SEQ42488.1, ECO:0000313|Proteomes:UP000198999};
RN [1] {ECO:0000313|EMBL:SEQ42488.1, ECO:0000313|Proteomes:UP000198999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21035 {ECO:0000313|EMBL:SEQ42488.1,
RC ECO:0000313|Proteomes:UP000198999};
RA de Groot N.N.;
RL Submitted (OCT-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; FOFN01000002; SEQ42488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9FYB0; -.
DR STRING; 419940.SAMN05421824_1607; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00046; UER00506.
DR Proteomes; UP000198999; 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00985};
KW Ligase {ECO:0000313|EMBL:SEQ42488.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00985}; Reference proteome {ECO:0000313|Proteomes:UP000198999};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00985}.
FT DOMAIN 43..385
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 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 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 395 AA; 43530 MW; 0851AF56AA4245A4 CRC64;
MYGAIKEQFK ADLNTIKESG LYKNERVITS KQGAEIDTLT NLDVLNFCAN NYLGLSSNDD
VIKAGIDTLN THGFGLSSVR FICGTQDIHK ELERKTAEFL GMEDCILYAA AFDANGGLFE
PILSKEDAII SDELNHASII DGVRLCKAQR FRYKNCDMVD LEAQLKAASS ARRKLIVTDG
SFSMDGKIAP LDKICDLADK YEALVMIDEC HSTGFIGKTG RGVHEYHNVM DRVDIITGTY
GKALGGASGG FTAARKEIVD ILRQHSRPYL FSNTLAPAIV GATLKVFDLI AEDTSLRDKL
EDNTKFFRTE MTKAGFDIIP GIHPIVPIML YDANLAQTFA KMLLDEGIYV IGFFYPVVPK
GKARIRVQLS AAHNKAHIQK AIDAFVKVGK KLEVI
//
