Reviewed, UniProtKB/Swiss-Prot O50584 (LTAE_PSEUN)

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:	ltaP

Organism

Pseudomonas sp. (strain NCIMB 10558)

Taxonomic identifier

268808 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. Can also act on L-erythro-phenylserine, L-threo-phenylserine, L-beta-3,4-methylenedioxyphenylserine and L-beta-3,4-dihydroxyphenylserine.
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 8.0-8.5. Temperature dependence: Optimum temperature is 25 degrees Celsius.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threonine aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 346	346	Low specificity L-threonine aldolase		PRO_0000121578
Amino acid modifications
	Modified residue	207	1	N6-(pyridoxal phosphate)lysine Probable
Experimental info
	Mutagenesis	207	1	K → A: Loss of activity. Ref.1
	Mutagenesis	207	1	K → R: 1000-fold decrease in activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O50584-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 9B2D6FDE002DB68D	FASTA	346	37,948
	10 20 30 40 50 60 MTDQSQQFAS DNYSGICPEA WAAMEKANHG HERAYGDDQW TARAADHFRK LFETDCEVFF 70 80 90 100 110 120 AFNGTAANSL ALSSLCQSYH SVICSETAHV ETDECGAPEF FSNGSKLLTA RSEGGKLTPA 130 140 150 160 170 180 SIREVALKRQ DIHYPKPRVV TITQATEVGS VYRPDELKAI SATCKELGLN LHMDGARFSN 190 200 210 220 230 240 ACAFLGCTPA ELTWKAGIDV LCFGGTKNGM AVGEAILFFN RKLAEDFDYR CKQAGQLASK 250 260 270 280 290 300 MRFLSAPWVG LLEDGAWLRH AAHANHCAQL LSSLVADIPG VELMFPVEAN GVFLQMSEPA 310 320 330 340 LEALRNKGWR FYTFIGSGGA RFMCSWDTEE ARVRELAADI RAVMSA

References

[1]

"Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558." Liu J.-Q., Ito S., Dairi T., Itoh N., Kataoka M., Shimizu S., Yamada H. Appl. Environ. Microbiol. 64:549-554(1998) [PubMed: 9464392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF LYS-207, CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB001577 Genomic DNA. Translation: BAA24794.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR001597. ArAA_b-elim_lyase/Thr_aldolase. 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_PSEUN

Accession

Primary (citable) accession number: O50584

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	June 1, 1998
Last modified:	September 22, 2009
This is version 40 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)