Detail Information for IndEnz0002009840
IED ID IndEnz0002009840
Enzyme Type ID protease009840
Protein Name Threonine dehydratase 2 biosynthetic, chloroplastic
EC 4.3.1.17
EC 4.3.1.19
SlTD2
Threonine deaminase 2

Cleaved into: Processed threonine dehydratase 2
Processed TD2
pTD2
Gene Name TD2 TD
Organism Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Solanales Solanaceae Solanoideae Solaneae Solanum Solanum subgen. Lycopersicon Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Enzyme Sequence MEFLCLAPTRSFSTNPKLTKSIPSDHTSTTSRIFTYQNMRGSTMRPLALPLKMSPIVSVPDITAPVENVPAILPKVVPGELIVNKPTGGDSDELFQYLVDILASPVYDVAIESPLELAEKLSDRLGVNFYIKREDKQRVFSFKLRGAYNMMSNLSREELDKGVITASAGNHAQGVALAGQRLNCVAKIVMPTTTPQIKIDAVRALGGDVVLYGKTFDEAQTHALELSEKDGLKYIPPFDDPGVIKGQGTIGTEINRQLKDIHAVFIPVGGGGLIAGVATFFKQIAPNTKIIGVEPYGAASMTLSLHEGHRVKLSNVDTFADGVAVALVGEYTFAKCQELIDGMVLVANDGISAAIKDVYDEGRNILETSGAVAIAGAAAYCEFYKIKNENIVAIASGANMDFSKLHKVTELAGLGSGKEALLATFMVEQQGSFKTFVGLVGSLNFTELTYRFTSERKNALILYRVNVDKESDLEKMIEDMKSSNMTTLNLSHNELVVDHLKHLVGGSANISDEIFGEFIVPEKAETLKTFLDAFSPRWNITLCRYRNQGDINASLLMGFQVPQAEMDEFKNQADKLGYPYELDNYNEAFNLVVSE
Enzyme Length 595
Uniprot Accession Number P25306
Absorption
Active Site
Activity Regulation ACTIVITY REGULATION: Threonine dehydratase 2 biosynthetic, chloroplastic: Strongly inhibited by 1 mM isoleucine (PubMed:21436043). Processed threonine dehydratase 2: Not inhibited by isoleucine (PubMed:21436043, PubMed:17416643). {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:21436043}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19; Evidence={ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:2011578, ECO:0000269|PubMed:21436043}; CATALYTIC ACTIVITY: Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17; Evidence={ECO:0000269|PubMed:17416643};
DNA Binding
EC Number 4.3.1.17; 4.3.1.19
Enzyme Function FUNCTION: [Threonine dehydratase 2 biosynthetic, chloroplastic]: Not required for normal growth and development of the plant (PubMed:21436043). {ECO:0000269|PubMed:21436043}.; FUNCTION: [Processed threonine dehydratase 2]: Involved in defense against lepidopteran, but not coleopteran herbivore insects (PubMed:21436043, PubMed:17416643). Acts in the insect gut to degrade threonine, which is an essential and limiting nutrient for the growth of lepidopteran larvae (Probable). Active against both L-threonine and L-serine (PubMed:17416643). {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:21436043, ECO:0000305}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Threonine dehydratase 2 biosynthetic, chloroplastic: Optimum temperature is 60 degrees Celsius. Abnormally stable at elevated temperatures (PubMed:21436043). Processed threonine dehydratase 2: Active over a wide range of temperatures. Optimal enzyme activity against L-threonine is at 58 degrees Celsius (PubMed:17416643). {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:21436043};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Threonine dehydratase 2 biosynthetic, chloroplastic: Active at alkaline pH (PubMed:21436043, PubMed:17416643). Processed threonine dehydratase 2: Optimum pH is 9. Has little or no activity at pH values below 6.0 (PubMed:17416643). {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:21436043};
Pathway PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
nucleotide Binding
Features Beta strand (12); Chain (2); Domain (2); Helix (20); Modified residue (1); Transit peptide (1)
Keywords 3D-structure;Amino-acid biosynthesis;Branched-chain amino acid biosynthesis;Chloroplast;Direct protein sequencing;Isoleucine biosynthesis;Lyase;Plant defense;Plastid;Pyridoxal phosphate;Reference proteome;Repeat;Transit peptide
Interact With Itself
Induction INDUCTION: Expression is induced in response to methyl jasmonate (MeJA) and locally and systemically in response to mechanical wounding (PubMed:17416643). Parenchyma-specific induction of expression in flowers and leaves by MeJA. No induction of expression by MeJA in epidermal, vascular or sporogenous tissues (PubMed:7550377). Caterpillar (Helicoverpa zea) labial saliva induces expression in leaves damaged by herbivory (PubMed:23065106). {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:23065106, ECO:0000269|PubMed:7550377}.
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
Modified Residue MOD_RES 143; /note=N6-(pyridoxal phosphate)lysine; /evidence=ECO:0000250|UniProtKB:P04968
Post Translational Modification PTM: Proteolytically cleaved by a chymotrypsin-like digestive protease in the midgut of the lepidopteran insects to remove the C-terminal regulatory domain, which allows efficient metabolizing of threonine in the presence of high isoleucine levels in the gut. {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:21436043}.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3IAU;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 64,937
Kinetics
Metal Binding
Rhea ID RHEA:22108; RHEA:19169
Cross Reference Brenda 4.3.1.19;