ID A0A1Y3WNB0_9BACT Unreviewed; 397 AA.
AC A0A1Y3WNB0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-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=B5G10_05275 {ECO:0000313|EMBL:OUN73208.1};
OS Barnesiella sp. An55.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=1965646 {ECO:0000313|EMBL:OUN73208.1, ECO:0000313|Proteomes:UP000196624};
RN [1] {ECO:0000313|Proteomes:UP000196624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An55 {ECO:0000313|Proteomes:UP000196624};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUN73208.1}.
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DR EMBL; NFHZ01000006; OUN73208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3WNB0; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00046; UER00506.
DR Proteomes; UP000196624; Unassembled WGS sequence.
DR GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:UniProtKB-UniRule.
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:SF102; 2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE, MITOCHONDRIAL; 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 Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985};
KW Reference proteome {ECO:0000313|Proteomes:UP000196624};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00985, ECO:0000313|EMBL:OUN73208.1}.
FT DOMAIN 45..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT BINDING 112..113
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 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
FT BINDING 184
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 240..243
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 273..274
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 367
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
SQ SEQUENCE 397 AA; 43806 MW; 0C1C9FFD99667369 CRC64;
MFTQMKEHLA KQLAEIKADG LYKEERTIIT PQSSAIRIAE KSGTVLNFCA NNYLGLSDNP
RLIAAAKKAM DTHGFGMSSV RFICGAQDLH RELEKAIARY FKTEDTILYA ACFDANGGVF
EPLFTAEDAI ISDALNHASI IDGVRLCKAK RYRYANANME ELEHCLQEAQ AQRFRIIVTD
GVFSMDGNVA PMDKICALAE KYDALVMVDE CHSAGVVGPH GRGVSELFNL YDRIDIHTGT
LGKAFGGAIG GFTTGPKEII DMLRQRSRPY LFSNSLPPAV VGAGIEVFKM LDESDELHTR
LVENVNYFRD KMLTAGFDIK PTQSAICAVM LYDAKLSQTF AAQMLDEGIY VTGFYYPVVP
QGQARIRVQL SAAHTREELD TCIAAFIKVA KNLGVLK
//