ID A0A1I4ZF06_9FLAO Unreviewed; 397 AA.
AC A0A1I4ZF06;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN04487989_101757 {ECO:0000313|EMBL:SFN48460.1};
OS Bizionia echini.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Bizionia.
OX NCBI_TaxID=649333 {ECO:0000313|EMBL:SFN48460.1, ECO:0000313|Proteomes:UP000198705};
RN [1] {ECO:0000313|EMBL:SFN48460.1, ECO:0000313|Proteomes:UP000198705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23925 {ECO:0000313|EMBL:SFN48460.1,
RC ECO:0000313|Proteomes:UP000198705};
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; FOVN01000001; SFN48460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4ZF06; -.
DR STRING; 649333.SAMN04487989_101757; -.
DR OrthoDB; 9807157at2; -.
DR UniPathway; UPA00046; UER00506.
DR Proteomes; UP000198705; 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:SFN48460.1};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00985}.
FT DOMAIN 43..386
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 185
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 241..244
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 274..275
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 368
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00985"
SQ SEQUENCE 397 AA; 43659 MW; 607D87445CE2F82E CRC64;
MYGKIQQHLE NELQEIKNNG LYKTERVITS AQGAEITLNT GETVLNFCAN NYLGLSSHPD
VIQAAKDVMD THGFGMSSVR FICGTQDIHK ELEQKIADFY GTEDTILYAA AFDANGGVFE
PLLEKEDAII SDSLNHASII DGVRLCKAAR YRYKNNDMAD LENQLIEANK NGARHKIIVT
DGVFSMDGLV APLDKICDLA DKYDALVMID ECHATGFIGK TGRGTLEEKG VMNRVDIITG
TLGKAMGGAM GGYTTAKKEV IEILRQRSRP YLFSNSLAPA IVGASIKVFD MLATDTTLRD
KLAWNTDYFK AGIKKAGFDI IDGDSAIVPI MLYDAKLSQT MANQLLKEGI YVIGFFFPVV
PKDKARIRVQ LSAAHEKEHL DQAISAFIKV GKELEII
//
