[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, AND CHARACTERIZATION. STRAIN=GS245, and K12 / ME9012; PubMed=9692922 [NCBI, ExPASy, EBI, Israel, Japan] Liu J.-Q., Dairi T., Itoh N., Kataoka M., Shimizu S., Yamada H.; "Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli."; Eur. J. Biochem. 255:220-226(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; DNA Res. 3:137-155(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

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.
CATALYTIC ACTIVITY: L-allo-threonine = glycine + acetaldehyde.
COFACTOR: Pyridoxal phosphate.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 8.5-9.0;
Temperature dependence: Optimum temperature is 65-70 degrees Celsius;
SUBUNIT: Homotetramer (Probable).
INTERACTION:
P18843:nadE; NbExp=1; IntAct=EBI-1120660, EBI-548960;
SIMILARITY: Belongs to the threonine aldolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB005050; BAA20882.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73957.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35584.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F64825; F64825.

RefSeq

AP_001501.1; -.
NP_415391.1; -.

3D structure databases

HSSP

Q9X266; 1M6S. [HSSP ENTRY / PDB]

ModBase

P75823.

Protein-protein interaction databases

IntAct

P75823; -.

Enzyme and pathway databases

BioCyc

EcoCyc:LTAA-MON; -.
MetaCyc:LTAA-MON; -.

Organism-specific databases

EchoBASE

EB3454; -.

EcoGene

EG13690; ltaE.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR001597; Beta_elim_lyase.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
IPR015422; PyrdxlP-dep_Trfase_major_sub2.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.

Pfam

PF01212; Beta_elim_lyase; 1.
Pfam graphical view of domain structure.

BLOCKS

P75823.

Genome annotation databases

GeneID

944955; -.

GenomeReviews

U00096_GR; b0870.
AP009048_GR; JW0854.

KEGG

ecj:JW0854; -.
eco:b0870; -.

Phylogenomic databases

HOGENOM

P75823; -.

Genome annotation databases

CMR

P75823; b0870.

Other

ProtoNet

P75823.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Direct protein sequencing; Lyase; Pyridoxal phosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 333`	`333`	`Low specificity L-threonine aldolase.`	`PRO_0000121575`
`BINDING`	`197 197`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 333 AA [This is the length of the unprocessed precursor]

Molecular weight: 36495 Da [This is the MW of the unprocessed precursor]

CRC64: 446C680A620083D9 [This is a checksum on the sequence]

        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

P75823 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools