ID A0A024HDJ3_PSEKB Unreviewed; 334 AA.
AC A0A024HDJ3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:CDF82961.1};
DE EC=4.1.2.48 {ECO:0000313|EMBL:CDF82961.1};
GN Name=ltae3 {ECO:0000313|EMBL:CDF82961.1};
GN ORFNames=PKB_1600 {ECO:0000313|EMBL:CDF82961.1};
OS Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF82961.1, ECO:0000313|Proteomes:UP000025241};
RN [1] {ECO:0000313|EMBL:CDF82961.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF82961.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Linke B.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDF82961.1, ECO:0000313|Proteomes:UP000025241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B13 {ECO:0000313|EMBL:CDF82961.1,
RC ECO:0000313|Proteomes:UP000025241};
RA Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA Roy S., Van der Meer J.R.;
RT "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL Submitted (MAY-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; HG322950; CDF82961.1; -; Genomic_DNA.
DR RefSeq; WP_043250566.1; NZ_HG322950.1.
DR AlphaFoldDB; A0A024HDJ3; -.
DR STRING; 1301098.PKB_1600; -.
DR KEGG; pkc:PKB_1600; -.
DR PATRIC; fig|1301098.3.peg.1594; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_3_6; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000025241; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:CDF82961.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000025241}.
FT DOMAIN 5..284
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 334 AA; 35560 MW; 55ACCE2F962A5383 CRC64;
MSVIDLRSDT VTLPTTGMRE AMARAELGDD VYGEDPTVNR LEATLAERLG FEAGLFVPTG
TMSNLLGLMA HCGRGDEYIV GQQAHTYKYE GGGAAVLGSI QPQPIDGEAD GSLDLAKVEA
AIKQDDFHFA RTRLLALENT MQGKVLPQSY LAAAREMTRR RGLGLHLDGA RLYNAAVKLG
VDAGEITRYF DSVSVCLSKG LGAPVGSVLC GSTELIGKAR RLRKMVGGGM RQAGGLAAAG
LYALDHQVER LAEDHVNAET LGRELAGLGY GIEPVQTNMV YVDIGAQASA LGAFLGERGI
RVSPAPRLRL VTHLDVKGTD IPHIVEAFAA FRRN
//