ID   TD_SOLTU                Reviewed;         359 AA.
AC   P31212;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Threonine dehydratase biosynthetic, chloroplastic {ECO:0000305};
DE            EC=4.3.1.19 {ECO:0000250|UniProtKB:P25306};
DE   AltName: Full=Threonine deaminase {ECO:0000305};
DE   Flags: Fragment;
GN   Name=TD {ECO:0000305};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Berolina {ECO:0000303|PubMed:1392612};
RC   TISSUE=Leaf {ECO:0000303|PubMed:1392612};
RX   PubMed=1392612; DOI=10.2307/3869484;
RA   Hildmann T., Ebneth M., Pena-Cortes H., Sanchez-Serrano J.J.,
RA   Willmitzer L., Prat S.;
RT   "General roles of abscisic and jasmonic acids in gene activation as a
RT   result of mechanical wounding.";
RL   Plant Cell 4:1157-1170(1992).
RN   [2]
RP   TISSUE SPECIFICITY.
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).
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:0000250|UniProtKB:P25306};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P04968};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P25306}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Floral buds of untreated plants. After ABA
CC       treatment or mechanical wounding is mostly accumulated in leaves, to a
CC       lesser extent in stems, but not in roots (PubMed:1392612). Expressed in
CC       anthers, carpel leaves, pith cells, sepals and petals. Not expressed in
CC       stomium, vascular bundles, epidermal cells or pollen mother cells
CC       (PubMed:7550377). {ECO:0000269|PubMed:1392612,
CC       ECO:0000269|PubMed:7550377}.
CC   -!- INDUCTION: By abscisic acid (ABA), jasmonic acid (JA) and wounding.
CC       {ECO:0000269|PubMed:1392612}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
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DR   EMBL; X67846; CAA48039.1; -; mRNA.
DR   PIR; PQ0468; PQ0468.
DR   AlphaFoldDB; P31212; -.
DR   SMR; P31212; -.
DR   STRING; 4113.PGSC0003DMT400033801; -.
DR   eggNOG; KOG1250; Eukaryota.
DR   InParanoid; P31212; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P31212; baseline.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR   GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR   GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.1020.10; -; 1.
DR   Gene3D; 3.40.50.1100; -; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR001721; TD_ACT-like.
DR   InterPro; IPR038110; TD_ACT-like_sf.
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; 1.
DR   PROSITE; PS51672; ACT_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Chloroplast; Isoleucine biosynthesis; Lyase; Plastid; Pyridoxal phosphate;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           <1..359
FT                   /note="Threonine dehydratase biosynthetic, chloroplastic"
FT                   /id="PRO_0000185581"
FT   DOMAIN          184..256
FT                   /note="ACT-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   DOMAIN          278..349
FT                   /note="ACT-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   NON_TER         1
SQ   SEQUENCE   359 AA;  39088 MW;  94DC75974AF9EA30 CRC64;
     PFDAPGVIKG QGTIGTEINR QLKDIHAVFV PVGGGGLISG VAAYFTQVAP HTKIIGVEPY
     GAASMTLSLY EGHRVKLENV DTFADGVAVA LVGEYTFAKC QELIDGMVLV RNDGISAAIK
     DVYDEGRNIL ETSGAVAIAG AAAYCEFYNI KNENIVAIAS GANMDFSKLH KVTELAELGS
     DNEALLATFM IEQPGSFKTF AKLVGSMNIT EVTYRFTSER KEALVLYRVD VDEKSDLEEM
     IKKLNSSNMK TFNFSHNELV AEHIKHLVGG SASISDEIFG EFIFPEKAGT LSTFLEAFSP
     RWNITLCRYR DQGDINGNVL VGFQVPQSEM DEFKSQADGL GYPYELDNSN EAFNIVVAE