ID   A0A157SKQ5_9BORD        Unreviewed;       337 AA.
AC   A0A157SKQ5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:SAI71058.1};
DE            EC=4.1.2.48 {ECO:0000313|EMBL:SAI71058.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:SAI71058.1};
GN   Name=ltaE {ECO:0000313|EMBL:SAI71058.1};
GN   ORFNames=SAMEA3906487_02600 {ECO:0000313|EMBL:SAI71058.1};
OS   Bordetella trematum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI71058.1, ECO:0000313|Proteomes:UP000076825};
RN   [1] {ECO:0000313|EMBL:SAI71058.1, ECO:0000313|Proteomes:UP000076825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H044680328 {ECO:0000313|EMBL:SAI71058.1,
RC   ECO:0000313|Proteomes:UP000076825};
RG   Pathogen Informatics;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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DR   EMBL; LT546645; SAI71058.1; -; Genomic_DNA.
DR   RefSeq; WP_025517856.1; NZ_UFUJ01000001.1.
DR   AlphaFoldDB; A0A157SKQ5; -.
DR   STRING; 123899.SAMEA3906487_02600; -.
DR   GeneID; 56590143; -.
DR   KEGG; btrm:SAMEA390648702600; -.
DR   PATRIC; fig|123899.6.peg.2588; -.
DR   eggNOG; COG2008; Bacteria.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000076825; Chromosome 1.
DR   GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:SAI71058.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076825}.
FT   DOMAIN          3..285
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   337 AA;  35565 MW;  D8F5F734B3662FBE CRC64;
     MIDFRSDTVT RPTAAMRQAM AQAPVGDDVM GDDPSVRALQ EAVAGRAGKE AGLFFPSGTQ
     SNLAALMAHC GRGDEYLAGQ QAHTYKFEGG GAAVLGSIQP QPIEHDADGS LPLARLAAAV
     KPVGDAHYAR TRLLALENTF HGKVIDQGYI LEAAAFARSR QLATHLDGAR VFNASVASGL
     SLAELCQPFD TVSICFSKGL GAPVGSVLVG SQALIDTARR WRKVLGGGMR QAGVLAAGAL
     HALDHHVERL AQDHEHARLL AEGLGGLPGV QVLSQQTNMV FVQFDPQRCA GLQDGLQAEG
     IAMRAVYGGP TRLVTHLDIS REDIARTVQT LARLLRA
//