ID   A0A0A8UXM6_LEGHA        Unreviewed;       342 AA.
AC   A0A0A8UXM6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:CEK11887.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:CEK11887.1};
GN   Name=ltaE {ECO:0000313|EMBL:CEK11887.1};
GN   ORFNames=LHA_2893 {ECO:0000313|EMBL:CEK11887.1};
OS   Legionella hackeliae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=449 {ECO:0000313|EMBL:CEK11887.1, ECO:0000313|Proteomes:UP000032803};
RN   [1] {ECO:0000313|Proteomes:UP000032803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC35250 {ECO:0000313|Proteomes:UP000032803};
RA   Gomez-Valero L.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the threonine aldolase family.
CC       {ECO:0000256|ARBA:ARBA00006966}.
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DR   EMBL; LN681225; CEK11887.1; -; Genomic_DNA.
DR   RefSeq; WP_045106990.1; NZ_UGOC01000002.1.
DR   AlphaFoldDB; A0A0A8UXM6; -.
DR   STRING; 449.LHA_2893; -.
DR   KEGG; lha:LHA_2893; -.
DR   PATRIC; fig|449.7.peg.1431; -.
DR   HOGENOM; CLU_029381_0_3_6; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000032803; Chromosome I.
DR   GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd06502; TA_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   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:CEK11887.1}.
FT   DOMAIN          5..286
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         199
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   342 AA;  37837 MW;  2C64A00F32E0EC46 CRC64;
     MKTIDLRSDT MTKPSHEMLQ VMMQAEVGDD VWGEDPTAKH LEALIADKAG MEAAVFAPSG
     TQSNLMGLMA HCERGDEYIV GQSAHTYRWE GGGAAVLGSI QPQPLDFASD GSLPLDKVTS
     AIKPWDDHHP RTKLLCLENT TDGKVVPLDY LQKIPQFCQE HQLKSHLDGA RVFNAVVKLQ
     VPLIEITKNF DSVSICLSKG LGAPVGSVLC GSKELIKRAR RWRKVLGGGM RQVGILAAAG
     IYALEQNIER LNQDHENAFA LASALAELDE VEVDEVSLQT NILFIRFKER YPELQDTLEK
     KGVFFPKQAN KQGFVRLVTH LDISKNDIAA IINEVKTFYK KC
//