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Protein

Low specificity L-threonine aldolase

Gene

ltaE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro-phenylserine are also good substrates.

Catalytic activityi

L-threonine = glycine + acetaldehyde.1 Publication
L-allo-threonine = glycine + acetaldehyde.1 Publication

Cofactori

pH dependencei

Optimum pH is 8.5-9.0.

Temperature dependencei

Optimum temperature is 65-70 degrees Celsius.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • L-allo-threonine aldolase activity Source: EcoCyc
  • phenylserine aldolase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:LTAA-MONOMER.
ECOL316407:JW0854-MONOMER.
MetaCyc:LTAA-MONOMER.
BRENDAi4.1.2.48. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Low specificity L-threonine aldolase (EC:4.1.2.48)
Short name:
Low specificity L-TA
Gene namesi
Name:ltaE
Synonyms:ybjU
Ordered Locus Names:b0870, JW0854
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13690. ltaE.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Low specificity L-threonine aldolasePRO_0000121575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

EPDiP75823.
PaxDbiP75823.
PRIDEiP75823.

Interactioni

Subunit structurei

Homotetramer.Curated

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1120660,EBI-1120660

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262099. 12 interactions.
IntActiP75823. 1 interaction.
STRINGi511145.b0870.

Structurei

Secondary structure

1
333
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93Combined sources
Helixi14 – 229Combined sources
Turni28 – 314Combined sources
Helixi34 – 4613Combined sources
Beta strandi50 – 567Combined sources
Helixi58 – 6912Combined sources
Beta strandi74 – 796Combined sources
Helixi83 – 864Combined sources
Helixi91 – 944Combined sources
Beta strandi99 – 1035Combined sources
Helixi113 – 1197Combined sources
Beta strandi129 – 13911Combined sources
Helixi146 – 15813Combined sources
Beta strandi162 – 1665Combined sources
Helixi170 – 1778Combined sources
Helixi182 – 1854Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi205 – 2095Combined sources
Helixi211 – 22414Combined sources
Helixi232 – 24413Combined sources
Helixi249 – 26517Combined sources
Beta strandi270 – 2745Combined sources
Beta strandi277 – 2815Combined sources
Helixi284 – 29512Combined sources
Turni296 – 2983Combined sources
Beta strandi304 – 3107Combined sources
Helixi317 – 33014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WLXX-ray2.51A/B1-333[»]
ProteinModelPortaliP75823.
SMRiP75823. Positions 1-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the threonine aldolase family.Curated

Phylogenomic databases

eggNOGiENOG4105C5W. Bacteria.
COG2008. LUCA.
HOGENOMiHOG000219824.
InParanoidiP75823.
KOiK01620.
OMAiTMTNQVA.
OrthoDBiEOG65N16K.
PhylomeDBiP75823.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

P75823-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDLRSDTVT RPSRAMLEAM MAAPVGDDVY GDDPTVNALQ DYAAELSGKE
60 70 80 90 100
AAIFLPTGTQ ANLVALLSHC ERGEEYIVGQ AAHNYLFEAG GAAVLGSIQP
110 120 130 140 150
QPIDAAADGT LPLDKVAMKI KPDDIHFART KLLSLENTHN GKVLPREYLK
160 170 180 190 200
EAWEFTRERN LALHVDGARI FNAVVAYGCE LKEITQYCDS FTICLSKGLG
210 220 230 240 250
TPVGSLLVGN RDYIKRAIRW RKMTGGGMRQ SGILAAAGIY ALKNNVARLQ
260 270 280 290 300
EDHDNAAWMA EQLREAGADV MRQDTNMLFV RVGEENAAAL GEYMKARNVL
310 320 330
INASPIVRLV THLDVSREQL AEVAAHWRAF LAR
Length:333
Mass (Da):36,495
Last modified:February 1, 1997 - v1
Checksum:i446C680A620083D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005050 Genomic DNA. Translation: BAA20882.1.
U00096 Genomic DNA. Translation: AAC73957.1.
AP009048 Genomic DNA. Translation: BAA35584.1.
PIRiF64825.
RefSeqiNP_415391.1. NC_000913.3.
WP_000566376.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73957; AAC73957; b0870.
BAA35584; BAA35584; BAA35584.
GeneIDi944955.
KEGGiecj:JW0854.
eco:b0870.
PATRICi32116947. VBIEscCol129921_0899.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005050 Genomic DNA. Translation: BAA20882.1.
U00096 Genomic DNA. Translation: AAC73957.1.
AP009048 Genomic DNA. Translation: BAA35584.1.
PIRiF64825.
RefSeqiNP_415391.1. NC_000913.3.
WP_000566376.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WLXX-ray2.51A/B1-333[»]
ProteinModelPortaliP75823.
SMRiP75823. Positions 1-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262099. 12 interactions.
IntActiP75823. 1 interaction.
STRINGi511145.b0870.

Proteomic databases

EPDiP75823.
PaxDbiP75823.
PRIDEiP75823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73957; AAC73957; b0870.
BAA35584; BAA35584; BAA35584.
GeneIDi944955.
KEGGiecj:JW0854.
eco:b0870.
PATRICi32116947. VBIEscCol129921_0899.

Organism-specific databases

EchoBASEiEB3454.
EcoGeneiEG13690. ltaE.

Phylogenomic databases

eggNOGiENOG4105C5W. Bacteria.
COG2008. LUCA.
HOGENOMiHOG000219824.
InParanoidiP75823.
KOiK01620.
OMAiTMTNQVA.
OrthoDBiEOG65N16K.
PhylomeDBiP75823.

Enzyme and pathway databases

BioCyciEcoCyc:LTAA-MONOMER.
ECOL316407:JW0854-MONOMER.
MetaCyc:LTAA-MONOMER.
BRENDAi4.1.2.48. 2026.

Miscellaneous databases

PROiP75823.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli."
    Liu J.-Q., Dairi T., Itoh N., Kataoka M., Shimizu S., Yamada H.
    Eur. J. Biochem. 255:220-226(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, CATALYTIC ACTIVITY, CHARACTERIZATION.
    Strain: GS245 and K12 / ME9012.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiLTAE_ECOLI
AccessioniPrimary (citable) accession number: P75823
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: March 16, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.