ID   THD1_SOLTU              Reviewed;         359 AA.
AC   P31212;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Threonine dehydratase biosynthetic;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
DE            Short=TD;
DE   Flags: Fragment;
GN   Name=TD;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   MEDLINE=93005746; PubMed=1392612; DOI=10.1105/tpc.4.9.1157;
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).
CC   -!- CATALYTIC ACTIVITY: L-threonine = 2-oxobutanoate + NH(3).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- ENZYME REGULATION: Allosterically inhibited by isoleucine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- TISSUE SPECIFICITY: Floral buds of untreated plants. After ABA
CC       treatment or mechanical wounding is mostly accumulated in leaves,
CC       to a lesser extent in stems, but not in roots.
CC   -!- INDUCTION: By abscisic acid (ABA), jasmonic acid (JA) and
CC       wounding.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X67846; CAA48039.1; -; mRNA.
DR   PIR; PQ0468; PQ0468.
DR   HSSP; P04968; 1TDJ.
DR   BRENDA; 4.3.1.19; 296.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR001926; PyrdxlP-dep_enz_bsu.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001721; Thr_deHydtase_C.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 2.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; PARTIAL.
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   Stress response.
FT   CHAIN        <1    359       Threonine dehydratase biosynthetic.
FT                                /FTId=PRO_0000185581.
FT   NON_TER       1      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
//