P75823 (LTAE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Low specificity L-threonine aldolase
Short name=Low specificity L-TA
EC=4.1.2.48

Gene names

Name:	ltaE
Synonyms:	ybjU
Ordered Locus Names:	b0870, JW0854

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	L-threonine = glycine + acetaldehyde. Ref.1 L-allo-threonine = glycine + acetaldehyde. Ref.1
Cofactor	Pyridoxal phosphate.
Subunit structure	Homotetramer Probable.
Sequence similarities	Belongs to the threonine aldolase family.
Biophysicochemical properties	pH dependence: Optimum pH is 8.5-9.0. Temperature dependence: Optimum temperature is 65-70 degrees Celsius.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycine biosynthetic process Inferred from genetic interaction Ref.1. Source: EcoCyc
Molecular_function	L-allo-threonine aldolase activity Inferred from direct assay Ref.1. Source: EcoCyc phenylserine aldolase activity Inferred from direct assay Ref.1. Source: EcoCyc pyridoxal phosphate binding Inferred from direct assay Ref.1. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-1120660,EBI-548960

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	Low specificity L-threonine aldolase		PRO_0000121575
Amino acid modifications
	Modified residue	197	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P75823 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 446C680A620083D9	FASTA	333	36,495
	10 20 30 40 50 60 MIDLRSDTVT RPSRAMLEAM MAAPVGDDVY GDDPTVNALQ DYAAELSGKE AAIFLPTGTQ 70 80 90 100 110 120 ANLVALLSHC ERGEEYIVGQ AAHNYLFEAG GAAVLGSIQP QPIDAAADGT LPLDKVAMKI 130 140 150 160 170 180 KPDDIHFART KLLSLENTHN GKVLPREYLK EAWEFTRERN LALHVDGARI FNAVVAYGCE 190 200 210 220 230 240 LKEITQYCDS FTICLSKGLG TPVGSLLVGN RDYIKRAIRW RKMTGGGMRQ SGILAAAGIY 250 260 270 280 290 300 ALKNNVARLQ EDHDNAAWMA EQLREAGADV MRQDTNMLFV RVGEENAAAL GEYMKARNVL 310 320 330 INASPIVRLV THLDVSREQL AEVAAHWRAF LAR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB005050 Genomic DNA. Translation: BAA20882.1. U00096 Genomic DNA. Translation: AAC73957.1. AP009048 Genomic DNA. Translation: BAA35584.1.
PIR	F64825.
RefSeq	NP_415391.1. NC_000913.2. YP_489143.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P75823.
SMR	P75823. Positions 1-322.
ModBase	Search...
Protein-protein interaction databases
IntAct	P75823. 1 interaction.
STRING	511145.b0870.
Proteomic databases
PaxDb	P75823.
PRIDE	P75823.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73957; AAC73957; b0870. BAA35584; BAA35584; BAA35584.
GeneID	12933105. 944955.
KEGG	ecj:Y75_p0843. eco:b0870.
PATRIC	32116947. VBIEscCol129921_0899.
Organism-specific databases
EchoBASE	EB3454.
EcoGene	EG13690. ltaE.
Phylogenomic databases
eggNOG	COG2008.
HOGENOM	HOG000219824.
KO	K01620.
OMA	RIVTHLD.
ProtClustDB	PRK10534.
Enzyme and pathway databases
BioCyc	EcoCyc:LTAA-MONOMER. ECOL316407:JW0854-MONOMER. MetaCyc:LTAA-MONOMER.
Gene expression databases
Genevestigator	P75823.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 1 hit.
InterPro	IPR001597. 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]
Pfam	PF01212. Beta_elim_lyase. 1 hit. [Graphical view]
PIRSF	PIRSF017617. Thr_aldolase. 1 hit.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LTAE_ECOLI

Accession

Primary (citable) accession number: P75823

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program