ID A0A0A2E238_9PORP Unreviewed; 396 AA.
AC A0A0A2E238;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=HQ37_01825 {ECO:0000313|EMBL:KGN71530.1};
OS Porphyromonas sp. COT-239 OH1446.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN71530.1, ECO:0000313|Proteomes:UP000030150};
RN [1] {ECO:0000313|EMBL:KGN71530.1, ECO:0000313|Proteomes:UP000030150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas sp. COT-239_OH1446 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN71530.1}.
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DR EMBL; JRAO01000009; KGN71530.1; -; Genomic_DNA.
DR RefSeq; WP_036879516.1; NZ_JRAO01000009.1.
DR AlphaFoldDB; A0A0A2E238; -.
DR STRING; 1515613.HQ37_01825; -.
DR eggNOG; COG0156; Bacteria.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00046; UER00506.
DR Proteomes; UP000030150; 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 ECO:0000313|EMBL:KGN71530.1}; Ligase {ECO:0000313|EMBL:KGN71530.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985};
KW Reference proteome {ECO:0000313|Proteomes:UP000030150};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00985, ECO:0000313|EMBL:KGN71530.1}.
FT DOMAIN 43..385
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 396 AA; 43613 MW; 2E4D997A31EE0AFA CRC64;
MYKAIKQHLQ SELDGIRQAG LYKQERIIIT PQSADIKVGQ GQPVVNFCAN NYLGLSDHPR
LIEAAKKAMD SHGFGMSSVR FICGTQDIHK ALERAIADYF KTEDTILYAA CFDANGGLFE
PLFGPEDAII SDALNHASII DGVRLCKAQR YRYANADMAD LERVLQEAQS ARFRIIVTDG
VFSMDGNVAP MDKICDLADK YDAMVMVDEC HSAGVVGPTG RGVAEQFNCY GRIDIHTGTL
GKAFGGAVGG FTTGPKEVID MLRQRSRPYL FSNSIPPAVV GAGLEVFKML EESSELHTKL
MKNVNYFRDK MIAAGFDIKP TQSAICAVML YDAKLSQDYA ARLLEEGIYV TGFYYPVVPK
GEARIRVQLS AAHEQHHLDH AIEAFIKVGR ELGVIK
//
