LTAE_ECOLI
ID LTAE_ECOLI Reviewed; 333 AA.
AC P75823;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Low specificity L-threonine aldolase;
DE Short=Low specificity L-TA;
DE EC=4.1.2.48;
GN Name=ltaE; Synonyms=ybjU; OrderedLocusNames=b0870, JW0854;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RC STRAIN=GS245, and K12 / ME9012;
RX PubMed=9692922; DOI=10.1046/j.1432-1327.1998.2550220.x;
RA Liu J.-Q., Dairi T., Itoh N., Kataoka M., Shimizu S., Yamada H.;
RT "Gene cloning, biochemical characterization and physiological role of a
RT thermostable low-specificity L-threonine aldolase from Escherichia coli.";
RL Eur. J. Biochem. 255:220-226(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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.
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 Evidence={ECO:0000269|PubMed:9692922};
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 Evidence={ECO:0000269|PubMed:9692922};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9.0.;
CC Temperature dependence:
CC Optimum temperature is 65-70 degrees Celsius.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC -!- INTERACTION:
CC P75823; P75823: ltaE; NbExp=2; IntAct=EBI-1120660, EBI-1120660;
CC -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
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DR EMBL; AB005050; BAA20882.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73957.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35584.1; -; Genomic_DNA.
DR PIR; F64825; F64825.
DR RefSeq; NP_415391.1; NC_000913.3.
DR RefSeq; WP_000566376.1; NZ_SSZK01000002.1.
DR PDB; 3WLX; X-ray; 2.51 A; A/B=1-333.
DR PDBsum; 3WLX; -.
DR AlphaFoldDB; P75823; -.
DR SMR; P75823; -.
DR BioGRID; 4262099; 22.
DR IntAct; P75823; 1.
DR MINT; P75823; -.
DR STRING; 511145.b0870; -.
DR jPOST; P75823; -.
DR PaxDb; P75823; -.
DR PRIDE; P75823; -.
DR EnsemblBacteria; AAC73957; AAC73957; b0870.
DR EnsemblBacteria; BAA35584; BAA35584; BAA35584.
DR GeneID; 944955; -.
DR KEGG; ecj:JW0854; -.
DR KEGG; eco:b0870; -.
DR PATRIC; fig|1411691.4.peg.1407; -.
DR EchoBASE; EB3454; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_3_6; -.
DR InParanoid; P75823; -.
DR OMA; NKGGGAC; -.
DR PhylomeDB; P75823; -.
DR BioCyc; EcoCyc:LTAA-MON; -.
DR BioCyc; MetaCyc:LTAA-MON; -.
DR BRENDA; 4.1.2.48; 2026.
DR PRO; PR:P75823; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IDA:EcoCyc.
DR GO; GO:0050179; F:phenylserine aldolase activity; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0006545; P:glycine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..333
FT /note="Low specificity L-threonine aldolase"
FT /id="PRO_0000121575"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:3WLX"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 249..265
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:3WLX"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:3WLX"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:3WLX"
FT HELIX 317..330
FT /evidence="ECO:0007829|PDB:3WLX"
SQ SEQUENCE 333 AA; 36495 MW; 446C680A620083D9 CRC64;
MIDLRSDTVT RPSRAMLEAM MAAPVGDDVY GDDPTVNALQ DYAAELSGKE AAIFLPTGTQ
ANLVALLSHC ERGEEYIVGQ AAHNYLFEAG GAAVLGSIQP QPIDAAADGT LPLDKVAMKI
KPDDIHFART KLLSLENTHN GKVLPREYLK EAWEFTRERN LALHVDGARI FNAVVAYGCE
LKEITQYCDS FTICLSKGLG TPVGSLLVGN RDYIKRAIRW RKMTGGGMRQ SGILAAAGIY
ALKNNVARLQ EDHDNAAWMA EQLREAGADV MRQDTNMLFV RVGEENAAAL GEYMKARNVL
INASPIVRLV THLDVSREQL AEVAAHWRAF LAR
