ID   TD_NICAT                Reviewed;         601 AA.
AC   Q9AXU4;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Threonine dehydratase {ECO:0000305};
DE            EC=4.3.1.19 {ECO:0000269|PubMed:17085687};
DE   AltName: Full=Threonine deaminase {ECO:0000303|PubMed:11161026};
DE   Flags: Precursor;
GN   Name=TD {ECO:0000303|PubMed:11161026};
GN   Synonyms=THD1 {ECO:0000312|EMBL:AAG59585.1};
GN   ORFNames=A4A49_00426 {ECO:0000312|EMBL:OIT01433.1};
OS   Nicotiana attenuata (Coyote tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=49451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=11161026; DOI=10.1104/pp.125.2.683;
RA   Hermsmeier D., Schittko U., Baldwin I.T.;
RT   "Molecular interactions between the specialist herbivore Manduca sexta
RT   (Lepidoptera, Sphingidae) and its natural host Nicotiana attenuata. I.
RT   Large-scale changes in the accumulation of growth- and defense-related
RT   plant mRNAs.";
RL   Plant Physiol. 125:683-700(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND43833696;
RA   Kang J.-H., Baldwin I.T.;
RT   "Isolation and characterization of the threonine deaminase promoter in
RT   Nicotiana attenuata.";
RL   Plant Sci. 171:435-440(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28536194; DOI=10.1073/pnas.1700073114;
RA   Xu S., Brockmoeller T., Navarro-Quezada A., Kuhl H., Gase K., Ling Z.,
RA   Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA   Timmermann B., Gaquerel E., Baldwin I.T.;
RT   "Wild tobacco genomes reveal the evolution of nicotine biosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:6133-6138(2017).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=17085687; DOI=10.1105/tpc.106.041103;
RA   Kang J.H., Wang L., Giri A., Baldwin I.T.;
RT   "Silencing threonine deaminase and JAR4 in Nicotiana attenuata impairs
RT   jasmonic acid-isoleucine-mediated defenses against Manduca sexta.";
RL   Plant Cell 18:3303-3320(2006).
CC   -!- FUNCTION: Catalyzes the conversion of threonine to alpha-keto butyrate
CC       in isoleucine (Ile) biosynthesis (PubMed:17085687). Required for JA-Ile
CC       biosynthesis, a signaling molecule involved in defense and resistance
CC       to the herbivore Manduca sexta caterpillars (PubMed:17085687).
CC       {ECO:0000269|PubMed:17085687}.
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:17085687};
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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- INDUCTION: Induced by methyl jasmonate and feeding with the herbivore
CC       Manduca sexta caterpillars. {ECO:0000269|PubMed:11161026}.
CC   -!- MISCELLANEOUS: Plants silencing TD exhibit a stunt growth phenotype.
CC       {ECO:0000269|PubMed:17085687}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
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DR   EMBL; AF229927; AAG59585.1; -; mRNA.
DR   EMBL; AY928105; AAX22214.1; -; Genomic_DNA.
DR   EMBL; MJEQ01037189; OIT01433.1; -; Genomic_DNA.
DR   RefSeq; XP_019250776.1; XM_019395231.1.
DR   AlphaFoldDB; Q9AXU4; -.
DR   SMR; Q9AXU4; -.
DR   STRING; 49451.Q9AXU4; -.
DR   EnsemblPlants; OIT01433; OIT01433; A4A49_00426.
DR   GeneID; 109229701; -.
DR   Gramene; OIT01433; OIT01433; A4A49_00426.
DR   KEGG; nau:109229701; -.
DR   OMA; YDEGRNI; -.
DR   OrthoDB; 906802at2759; -.
DR   BRENDA; 4.3.1.19; 9729.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000187609; Chromosome 7.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.
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   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Chloroplast; Isoleucine biosynthesis; Lyase; Plant defense; Plastid;
KW   Pyridoxal phosphate; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           52..601
FT                   /note="Threonine dehydratase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000446308"
FT   DOMAIN          427..499
FT                   /note="ACT-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   DOMAIN          521..592
FT                   /note="ACT-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
SQ   SEQUENCE   601 AA;  65645 MW;  54B9EA06D9053896 CRC64;
     MEVLCQAPAG NSNFACNPKF TAIRTRAISS NDTFKVISST GNNKKMKGAI RTSIPKPSAL
     PLKVSQLSPS ADSMPVPASL QDVEAGKLIE NNPSGGDTEE LFQYLVEILA SRVYDVAIDS
     PLQNAAKLSK KLGVNFWIKR EDMQSVFSFK LRGAYNMMTK LSKEQLERGV ITASAGNHAQ
     GVALGAQRLK CTATIVMPVT TPEIKIEAVK NLDGKVVLHG DTFDKAQEHA LKLAEDEGLT
     FIPPFDHPDV IIGQGTIGTE INRQLKDIHA VFVPVGGGGL IAGVAAYFKR VAPHTKIIGV
     EPFGASSMTQ SLYHGERVKL EQVDNFADGV AVALVGEETF RLCKDLIDGM VLVSNDAISA
     AVKDVYDEGR NILETSGALA IAGAEAYCKY YNIKGENVVA IASGANMDFS KLKLVVDLAD
     IGGQREALLA TFMPEEPGSF KKFCELVGPM NITEFKYRYN SGRKQALVLY SVGVNTKSDL
     ESMLERMKSS QLNTVNLTNN NLVKEHLRHL MGGRSEPSNE IFCQFIFPEK PGALRKFLDA
     FSPRWNISLF HYREQGELDA SVLVGFQVPK GEIEEFRVQA NNLGYSYEIE SLNEASQLIM
     E