Reviewed, UniProtKB/Swiss-Prot P75823 (LTAE_ECOLI)

Names and origin

Protein names

Recommended name:
    Low specificity L-threonine aldolase
      Short name=Low specificity L-TA
    EC=4.1.2.5

Gene names

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

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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. L-allo-threonine = glycine + acetaldehyde.
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
Gene Ontology (GO)
Biological process	glycine biosynthetic process Ref.1 Inferred from genetic interaction. Source: UniProtKB
Molecular function	L-allo-threonine aldolase activity Ref.1 Inferred from direct assay. Source: UniProtKB phenylserine aldolase activity Ref.1 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
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)
	P75823-1 [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: 9692922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, 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: 8905232] [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: 9278503] [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: 16738553] [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	AP_001501.1. NP_415391.1.
3D structure databases
SMR	P75823. Positions 1-332.
ModBase	Search...
Protein-protein interaction databases
IntAct	P75823. 1 interaction.
STRING	P75823.
Genome annotation databases
GeneID	944955.
GenomeReviews	Gene locus JW0854 in contig AP009048_GR. Gene locus b0870 in contig U00096_GR.
KEGG	ecj:JW0854. eco:b0870.
Organism-specific databases
EchoBASE	EB3454.
EcoGene	EG13690. ltaE.
CMR	Search...
Phylogenomic databases
eggNOG	COG2008.
HOGENOM	HBG293912.
OMA	GLKIHLD.
Enzyme and pathway databases
BioCyc	EcoCyc:LTAA-MONOMER. ECOL168927:B0870-MONOMER. MetaCyc:LTAA-MONOMER.
Gene expression databases
Genevestigator	P75823.
Family and domain databases
InterPro	IPR001597. ArAA_b-elim_lyase/Thr_aldolase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
Pfam	PF01212. Beta_elim_lyase. 1 hit. [Graphical view]
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:	February 9, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)