TD2_SOLLC
ID TD2_SOLLC Reviewed; 595 AA.
AC P25306;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Threonine dehydratase 2 biosynthetic, chloroplastic {ECO:0000305};
DE EC=4.3.1.17 {ECO:0000269|PubMed:17416643};
DE EC=4.3.1.19 {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:2011578, ECO:0000269|PubMed:21436043};
DE AltName: Full=SlTD2 {ECO:0000303|PubMed:17416643};
DE AltName: Full=Threonine deaminase 2 {ECO:0000303|PubMed:21436043};
DE Contains:
DE RecName: Full=Processed threonine dehydratase 2 {ECO:0000305};
DE AltName: Full=Processed TD2 {ECO:0000303|PubMed:17416643};
DE Short=pTD2 {ECO:0000303|PubMed:17416643, ECO:0000303|PubMed:21436043};
DE Flags: Precursor;
GN Name=TD2 {ECO:0000303|PubMed:21436043};
GN Synonyms=TD {ECO:0000303|PubMed:2011578};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF 2-595,
RP PROTEIN SEQUENCE OF 52-61, CATALYTIC ACTIVITY, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Tiny tim {ECO:0000303|PubMed:2011578};
RX PubMed=2011578; DOI=10.1073/pnas.88.7.2678;
RA Samach A., Hareven D., Gutfinger T., Ken-Dror S., Lifschitz E.;
RT "Biosynthetic threonine deaminase gene of tomato: isolation, structure, and
RT upregulation in floral organs.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2678-2682(1991).
RN [2]
RP PROTEIN SEQUENCE OF 52-75; 86-120; 146-181; 188-198; 205-233; 236-310;
RP 313-404 AND 408-418, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16357201; DOI=10.1073/pnas.0509026102;
RA Chen H., Wilkerson C.G., Kuchar J.A., Phinney B.S., Howe G.A.;
RT "Jasmonate-inducible plant enzymes degrade essential amino acids in the
RT herbivore midgut.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:19237-19242(2005).
RN [3] {ECO:0007744|PDB:3IAU}
RP PROTEIN SEQUENCE OF 53-75; 125-132; 139-143; 146-181; 188-198; 204-256;
RP 283-310; 313-404 AND 408-418, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, PTM, AND X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF
RP 53-418.
RC STRAIN=cv. MicroTom {ECO:0000303|PubMed:21436043};
RX PubMed=21436043; DOI=10.1073/pnas.1016157108;
RA Gonzales-Vigil E., Bianchetti C.M., Phillips G.N. Jr., Howe G.A.;
RT "Adaptive evolution of threonine deaminase in plant defense against insect
RT herbivores.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5897-5902(2011).
RN [4]
RP PROTEIN SEQUENCE OF 54-75; 103-120; 146-181; 188-198; 204-233; 246-256;
RP 260-282; 313-404 AND 408-418, IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, INDUCTION, AND PTM.
RC STRAIN=cv. Castlemart {ECO:0000303|PubMed:17416643};
RX PubMed=17416643; DOI=10.1104/pp.107.095588;
RA Chen H., Gonzales-Vigil E., Wilkerson C.G., Howe G.A.;
RT "Stability of plant defense proteins in the gut of insect herbivores.";
RL Plant Physiol. 143:1954-1967(2007).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=7550377; DOI=10.1046/j.1365-313x.1995.08030391.x;
RA Samach A., Broday L., Hareven D., Lifschitz E.;
RT "Expression of an amino acid biosynthesis gene in tomato flowers:
RT developmental upregulation and MeJa response are parenchyma-specific and
RT mutually compatible.";
RL Plant J. 8:391-406(1995).
RN [6]
RP INDUCTION.
RX PubMed=23065106; DOI=10.1007/s10886-012-0198-3;
RA Musser R.O., Hum-Musser S.M., Lee H.K., DesRochers B.L., Williams S.A.,
RA Vogel H.;
RT "Caterpillar labial saliva alters tomato plant gene expression.";
RL J. Chem. Ecol. 38:1387-1401(2012).
CC -!- FUNCTION: [Threonine dehydratase 2 biosynthetic, chloroplastic]: Not
CC required for normal growth and development of the plant
CC (PubMed:21436043). {ECO:0000269|PubMed:21436043}.
CC -!- FUNCTION: [Processed threonine dehydratase 2]: Involved in defense
CC against lepidopteran, but not coleopteran herbivore insects
CC (PubMed:21436043, PubMed:17416643). Acts in the insect gut to degrade
CC threonine, which is an essential and limiting nutrient for the growth
CC of lepidopteran larvae (Probable). Active against both L-threonine and
CC L-serine (PubMed:17416643). {ECO:0000269|PubMed:17416643,
CC ECO:0000269|PubMed:21436043, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC Evidence={ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:2011578,
CC ECO:0000269|PubMed:21436043};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC Evidence={ECO:0000269|PubMed:17416643};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P04968};
CC -!- ACTIVITY REGULATION: Threonine dehydratase 2 biosynthetic,
CC chloroplastic: Strongly inhibited by 1 mM isoleucine (PubMed:21436043).
CC Processed threonine dehydratase 2: Not inhibited by isoleucine
CC (PubMed:21436043, PubMed:17416643). {ECO:0000269|PubMed:17416643,
CC ECO:0000269|PubMed:21436043}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Threonine dehydratase 2 biosynthetic, chloroplastic: Active at
CC alkaline pH (PubMed:21436043, PubMed:17416643). Processed threonine
CC dehydratase 2: Optimum pH is 9. Has little or no activity at pH
CC values below 6.0 (PubMed:17416643). {ECO:0000269|PubMed:17416643,
CC ECO:0000269|PubMed:21436043};
CC Temperature dependence:
CC Threonine dehydratase 2 biosynthetic, chloroplastic: Optimum
CC temperature is 60 degrees Celsius. Abnormally stable at elevated
CC temperatures (PubMed:21436043). Processed threonine dehydratase 2:
CC Active over a wide range of temperatures. Optimal enzyme activity
CC against L-threonine is at 58 degrees Celsius (PubMed:17416643).
CC {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:21436043};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:2011578,
CC ECO:0000269|PubMed:21436043}.
CC -!- INTERACTION:
CC P25306; P25306: TD2; NbExp=2; IntAct=EBI-15916506, EBI-15916506;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in floral buds, 8-9 mm long flowers 1 to
CC 2 days before anthesis, open flowers and floral organs including
CC sepals, petals, stamens and carpels of 8-9 mm flowers (at protein
CC level) (PubMed:7550377). Expressed in very early floral meristems of
CC the anantha. Over 500-fold expression in mature flowers compared to
CC leaves (PubMed:2011578). Expressed in sepals, petals, stamens and
CC carpels of the mature flower. In sepals, mostly expressed in the
CC abaxial mesophyll cells and in petals in parenchymal cells. Not
CC expressed in epidermal or vascular tissues of sepals and petals. In
CC stamens, expressed in parenchymal cells of the connective and lobes,
CC but not expressed in differentiated tissues such as tapetum (TP),
CC stomium (SM), or pollen grains (PG) (PubMed:2011578, PubMed:7550377).
CC Not expressed in roots or seeds (PubMed:2011578). High level of
CC expression in immature flower buds, unopened flowers and opened flowers
CC (PubMed:17416643, PubMed:7550377). Not expressed in unstressed leaves,
CC root, stem or petiole (PubMed:17416643). {ECO:0000269|PubMed:17416643,
CC ECO:0000269|PubMed:2011578, ECO:0000269|PubMed:7550377}.
CC -!- DEVELOPMENTAL STAGE: During the pre-organogenesis stage of the floral
CC primordium, expressed in scattered islands of cells in the central
CC parenchymatous pith region and in the peripheral ground parenchyma.
CC Upon sepal buttresses emergence, expressed in all parenchyma mesophyll
CC cells accumulating in a continous pattern in the central pith cells of
CC the floral primordia, but not expressed in the future epidermal cells.
CC As the mesophyll and vascular tissues elongate and differentiate,
CC highly expressed in the abaxial mesophyll cells of sepals, but down-
CC regulated in the adaxial cell layers. At anthesis, down-regulated
CC expression in all mesophyll cells of the sepal. In petals, expressed in
CC all mesophyll cells throughout development.
CC {ECO:0000269|PubMed:7550377}.
CC -!- INDUCTION: Expression is induced in response to methyl jasmonate (MeJA)
CC and locally and systemically in response to mechanical wounding
CC (PubMed:17416643). Parenchyma-specific induction of expression in
CC flowers and leaves by MeJA. No induction of expression by MeJA in
CC epidermal, vascular or sporogenous tissues (PubMed:7550377).
CC Caterpillar (Helicoverpa zea) labial saliva induces expression in
CC leaves damaged by herbivory (PubMed:23065106).
CC {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:23065106,
CC ECO:0000269|PubMed:7550377}.
CC -!- PTM: Proteolytically cleaved by a chymotrypsin-like digestive protease
CC in the midgut of the lepidopteran insects to remove the C-terminal
CC regulatory domain, which allows efficient metabolizing of threonine in
CC the presence of high isoleucine levels in the gut.
CC {ECO:0000269|PubMed:17416643, ECO:0000269|PubMed:21436043}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; M61914; AAA34171.1; -; mRNA.
DR EMBL; M61915; AAA68097.1; -; Genomic_DNA.
DR PIR; A38628; A38628.
DR RefSeq; NP_001296095.1; NM_001309166.1.
DR PDB; 3IAU; X-ray; 2.35 A; A/B=53-418.
DR PDBsum; 3IAU; -.
DR AlphaFoldDB; P25306; -.
DR SMR; P25306; -.
DR DIP; DIP-59625N; -.
DR STRING; 4081.Solyc09g008670.2.1; -.
DR PaxDb; P25306; -.
DR PRIDE; P25306; -.
DR EnsemblPlants; Solyc09g008670.3.1; Solyc09g008670.3.1; Solyc09g008670.3.
DR GeneID; 543983; -.
DR Gramene; Solyc09g008670.3.1; Solyc09g008670.3.1; Solyc09g008670.3.
DR KEGG; sly:543983; -.
DR eggNOG; KOG1250; Eukaryota.
DR HOGENOM; CLU_021152_6_3_1; -.
DR InParanoid; P25306; -.
DR OMA; YDEGRNI; -.
DR OrthoDB; 906802at2759; -.
DR PhylomeDB; P25306; -.
DR BRENDA; 4.3.1.19; 3101.
DR UniPathway; UPA00047; UER00054.
DR EvolutionaryTrace; P25306; -.
DR Proteomes; UP000004994; Chromosome 9.
DR ExpressionAtlas; P25306; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0002213; P:defense response to insect; IDA:UniProtKB.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006565; P:L-serine catabolic process; IDA:UniProtKB.
DR GO; GO:0031349; P:positive regulation of defense response; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IDA:UniProtKB.
DR GO; GO:0009625; P:response to insect; IDA:UniProtKB.
DR GO; GO:0006567; P:threonine catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.1020.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001721; TD_ACT-like.
DR InterPro; IPR038110; TD_ACT-like_sf.
DR InterPro; IPR005787; Thr_deHydtase_biosynth.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 2.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR PROSITE; PS51672; ACT_LIKE; 2.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Chloroplast;
KW Direct protein sequencing; Isoleucine biosynthesis; Lyase; Plant defense;
KW Plastid; Pyridoxal phosphate; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:16357201,
FT ECO:0000269|PubMed:2011578"
FT CHAIN 52..595
FT /note="Threonine dehydratase 2 biosynthetic, chloroplastic"
FT /evidence="ECO:0000305|PubMed:16357201,
FT ECO:0000305|PubMed:2011578"
FT /id="PRO_0000033614"
FT CHAIN 52..415
FT /note="Processed threonine dehydratase 2"
FT /evidence="ECO:0000305|PubMed:17416643"
FT /id="PRO_0000445516"
FT DOMAIN 420..492
FT /note="ACT-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT DOMAIN 514..585
FT /note="ACT-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT MOD_RES 143
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P04968"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 216..230
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 241..257
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 288..295
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 368..383
FT /evidence="ECO:0007829|PDB:3IAU"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:3IAU"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:3IAU"
SQ SEQUENCE 595 AA; 64937 MW; AC430BB5DD9F0348 CRC64;
MEFLCLAPTR SFSTNPKLTK SIPSDHTSTT SRIFTYQNMR GSTMRPLALP LKMSPIVSVP
DITAPVENVP AILPKVVPGE LIVNKPTGGD SDELFQYLVD ILASPVYDVA IESPLELAEK
LSDRLGVNFY IKREDKQRVF SFKLRGAYNM MSNLSREELD KGVITASAGN HAQGVALAGQ
RLNCVAKIVM PTTTPQIKID AVRALGGDVV LYGKTFDEAQ THALELSEKD GLKYIPPFDD
PGVIKGQGTI GTEINRQLKD IHAVFIPVGG GGLIAGVATF FKQIAPNTKI IGVEPYGAAS
MTLSLHEGHR VKLSNVDTFA DGVAVALVGE YTFAKCQELI DGMVLVANDG ISAAIKDVYD
EGRNILETSG AVAIAGAAAY CEFYKIKNEN IVAIASGANM DFSKLHKVTE LAGLGSGKEA
LLATFMVEQQ GSFKTFVGLV GSLNFTELTY RFTSERKNAL ILYRVNVDKE SDLEKMIEDM
KSSNMTTLNL SHNELVVDHL KHLVGGSANI SDEIFGEFIV PEKAETLKTF LDAFSPRWNI
TLCRYRNQGD INASLLMGFQ VPQAEMDEFK NQADKLGYPY ELDNYNEAFN LVVSE
