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Database: UniProt
Entry: A0A1Y3WNB0_9BACT
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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
//
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