ID   A0A1M6Z9W6_9FLAO        Unreviewed;       397 AA.
AC   A0A1M6Z9W6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   22-NOV-2017, entry version 7.
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=SAMN05444366_0179 {ECO:0000313|EMBL:SHL27242.1};
OS   Flavobacterium saccharophilum.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=29534 {ECO:0000313|EMBL:SHL27242.1, ECO:0000313|Proteomes:UP000184121};
RN   [1] {ECO:0000313|EMBL:SHL27242.1, ECO:0000313|Proteomes:UP000184121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1811 {ECO:0000313|EMBL:SHL27242.1,
RC   ECO:0000313|Proteomes:UP000184121};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to
CC       glycine and acetyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00985}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + glycine = CoA + 2-amino-3-
CC       oxobutanoate. {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
CC       oxydo-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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00985}.
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DR   EMBL; FRBY01000001; SHL27242.1; -; Genomic_DNA.
DR   RefSeq; WP_072969785.1; NZ_FRBY01000001.1.
DR   GeneID; 33996368; -.
DR   UniPathway; UPA00046; UER00506.
DR   Proteomes; UP000184121; 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   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR13693:SF60; PTHR13693:SF60; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01822; 2am3keto_CoA; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00985};
KW   Complete proteome {ECO:0000313|Proteomes:UP000184121};
KW   Ligase {ECO:0000313|EMBL:SHL27242.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00985};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00985}.
FT   DOMAIN       43    386       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
FT   REGION      241    244       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00985}.
FT   REGION      274    275       Pyridoxal phosphate binding; shared with
FT                                dimeric partner. {ECO:0000256|HAMAP-Rule:
FT                                MF_00985}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00985}.
FT   BINDING     185    185       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00985}.
FT   BINDING     368    368       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00985}.
FT   MOD_RES     244    244       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00985}.
SQ   SEQUENCE   397 AA;  43461 MW;  F8CB79B910F109B6 CRC64;
     MYGKIKEHLQ NELQTIEESG IFKKERIITS EQGAEITIST GETVLNFCAN NYLGLSSHPE
     VVQAAKDTMD THGFGMSSVR FICGTQDIHK TLEKKIADFY GTEDTILYAA AFDANGGVFE
     PLLGENDAII SDSLNHASII DGVRLCKAAR YRYENSNMED LEQQLIKANE AGARFKLIVT
     DGVFSMDGLV APLDKICDLA DKYDAMVMVD ECHAAGFIGA TGKGTLEAKG VMGRVDIITG
     TLGKALGGAM GGYTTAKKEI IELLRQRSRP YLFSNSLAPA IVGASIKVFE LLEKDTSLRD
     KLEWNTNYFK QGMKEAGFDI IDGDSAIVPV MLYDAKLSQT MANELLNEGI YVIGFFFPVV
     PKEKARIRVQ LSAAHSKEHL DKAISAFKVV GQKLKVI
//