ID   LTAE_ECO57              Reviewed;         333 AA.
AC   P58319;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Low specificity L-threonine aldolase;
DE            Short=Low-specificity L-TA;
DE            EC=4.1.2.48;
GN   Name=ltaE; OrderedLocusNames=Z1104, ECs0956;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to
CC       glycine and acetaldehyde. L-threo-phenylserine and L-erythro-
CC       phenylserine are also good substrates (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:19625,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57926; EC=4.1.2.48;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-allo-threonine = acetaldehyde + glycine;
CC         Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:58585; EC=4.1.2.48;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG55252.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34379.1; -; Genomic_DNA.
DR   PIR; D90748; D90748.
DR   PIR; H85598; H85598.
DR   RefSeq; NP_308983.1; NC_002695.1.
DR   RefSeq; WP_000566359.1; NZ_SEKU01000006.1.
DR   AlphaFoldDB; P58319; -.
DR   SMR; P58319; -.
DR   STRING; 155864.EDL933_1004; -.
DR   EnsemblBacteria; AAG55252; AAG55252; Z1104.
DR   EnsemblBacteria; BAB34379; BAB34379; ECs_0956.
DR   GeneID; 917698; -.
DR   KEGG; ece:Z1104; -.
DR   KEGG; ecs:ECs_0956; -.
DR   PATRIC; fig|386585.9.peg.1072; -.
DR   eggNOG; COG2008; Bacteria.
DR   HOGENOM; CLU_029381_0_3_6; -.
DR   OMA; NKGGGAC; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008732; F:L-allo-threonine aldolase activity; IEA:RHEA.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR023603; Low_specificity_L-TA.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR48097:SF9; PTHR48097:SF9; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..333
FT                   /note="Low specificity L-threonine aldolase"
FT                   /id="PRO_0000121576"
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  36483 MW;  089512C8329671B8 CRC64;
     MIDLRSDTVT RPSRAMLEAM MAAPVGDDVY GDDPTVNALQ DYAAELSGKE AAIFLPTGTQ
     ANLVALLSHC ERGEEYIVGQ AAHNYLFEAG GAAVLGSIQP QPIDAAADGT LPLDKVAMKI
     KPDDIHFART KLLSLENTHN GKVLPREYLK DAWEFTRERN LALHVDGARI FNAVVAYGSE
     LKELTQYCDS FTICLSKGLG TPVGSLLVGN RDYIKRAIRW RKMTGGGMRQ SGILAAAGMY
     ALKNNVARLQ EDHDNAAWMA EQLREAGADV MRQDTNMLFV RVGEENAAAL GEYMKARNVL
     INASPIVRLV THLDVSREQL AEVAAHWRAF LAR