ID   THD1_CICAR              Reviewed;         590 AA.
AC   Q39469;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Threonine dehydratase biosynthetic, chloroplastic;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
DE            Short=TD;
DE   Flags: Precursor;
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Pusa 261 / PCITD 2; TISSUE=Seed;
RX   PubMed=7716234; DOI=10.1104/pp.107.3.1023;
RA   John S.J., Srivastava V., Guha-Mukherjee S.;
RT   "Cloning and sequencing of chickpea cDNA coding for threonine deaminase.";
RL   Plant Physiol. 107:1023-1024(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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Allosterically inhibited by isoleucine.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Found at higher levels in flowers than in other
CC       organs.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
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DR   EMBL; X78575; CAA55313.1; -; mRNA.
DR   PIR; T09532; T09532.
DR   AlphaFoldDB; Q39469; -.
DR   SMR; Q39469; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000087171; Genome assembly.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
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; 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.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Chloroplast;
KW   Isoleucine biosynthesis; Lyase; Plastid; Pyridoxal phosphate;
KW   Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..44
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..590
FT                   /note="Threonine dehydratase biosynthetic, chloroplastic"
FT                   /id="PRO_0000033613"
FT   DOMAIN          416..488
FT                   /note="ACT-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   DOMAIN          509..580
FT                   /note="ACT-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   MOD_RES         139
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   590 AA;  65153 MW;  01D7736AC92BCDEA CRC64;
     MLSTSTTNSS ILPFRSRASS STFIARPPAN FNSIFTTSVR VFPISMSRYC VFPHTWERDH
     NVPGVPGVLR KVVPAAPIKN KPTCADSDEL PEYLRDVLRS PVYDVVVESP VELTERLSDR
     LGVNFYVKRE DRQRVFSFKL RGPYNMMSSL SHEEIDKGVI TASAGNHAQG VPFPFPGRRL
     KCVAKIVMPT TTPNIKLDGV RALGADVVLW GHTFDEAKTH AVELCEKDGL RTIPPFEDPA
     VIKGQGTIGS EINRQIKRID AVFVPVGGGG LIAGVAAFFK QIAPQTKIIV VEPYDAASMA
     LSVHAEHRAK LSNVDTFADG ATVAVIGEYT FARCQDVVDA MVLVANDGIG AAIKDVFDEG
     RNIVETSGAA GIAGMYCEMY RIKNDNMVGI VSGANMNFRK LHKVSELAVL GSGHEALLGT
     YMPGQKGCFK TMAGLVHGSL SFTEITYRFT SHRRSILVLM LKLEPWRYIE KMIEMMKYSG
     VTVLNISHNE LAVIHGKHLV GGSAKVSDEV FVEFIIPEKA DLKKFLEVLS PHWNLTLYRY
     RNQGDLKATI LMVIASFLCE IVIRKNQIDD LGYPYEIDQY NDAFNLAVTE