NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Desiree;
TISSUE=Leaf;
DOI=10.1105/tpc.4.9.1157; PubMed=1392612 [NCBI, ExPASy, EBI, Israel, Japan]
Hildmann T., Ebneth M., Pena-Cortes H., Sanchez-Serrano J.J., Willmitzer L., Prat S.;
"General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding.";
Plant Cell 4:1157-1170(1992).

Comments

CATALYTIC ACTIVITY: L-threonine = 2-oxobutanoate + NH₃.
COFACTOR: Pyridoxal phosphate.
ENZYME REGULATION: Allosterically inhibited by isoleucine.
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Plastid, chloroplast.
TISSUE SPECIFICITY: Floral buds of untreated plants. After ABA treatment or mechanical wounding is mostly accumulated in leaves, to a lesser extent in stems, but not in roots.
INDUCTION: By abscisic acid (ABA), jasmonic acid (JA) and wounding.
SIMILARITY: Belongs to the serine/threonine dehydratase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X67846; CAA48039.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

PQ0468; PQ0468.

3D structure databases

HSSP

P04968; 1TDJ. [HSSP ENTRY / PDB]

ModBase

P31212.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0004794;	Molecular function: L-threonine ammonia-lyase activity (inferred from electronic annotation from InterPro).
GO:0030170;	Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0009097;	Biological process: isoleucine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006950;	Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001926; PyrdxlP-dep_enz_bsu.
IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001721; Thr_deHydtase_C.
Graphical view of domain structure.

Pfam

PF00291; PALP; 1.
PF00585; Thr_dehydrat_C; 2.
Pfam graphical view of domain structure.

PROSITE

PS00165; DEHYDRATASE_SER_THR; PARTIAL.

Other

ProtoNet

P31212.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allosteric enzyme; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Chloroplast; Isoleucine biosynthesis; Lyase; Plastid; Pyridoxal phosphate; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 359`	`>359`	`Threonine dehydratase biosynthetic.`	`PRO_0000185581`
`NON_TER`	`1 1`

Sequence information

Length: 359 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 39088 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 94DC75974AF9EA30 [This is a checksum on the sequence]

        10         20         30         40         50         60 
PFDAPGVIKG QGTIGTEINR QLKDIHAVFV PVGGGGLISG VAAYFTQVAP HTKIIGVEPY 

        70         80         90        100        110        120 
GAASMTLSLY EGHRVKLENV DTFADGVAVA LVGEYTFAKC QELIDGMVLV RNDGISAAIK 

       130        140        150        160        170        180 
DVYDEGRNIL ETSGAVAIAG AAAYCEFYNI KNENIVAIAS GANMDFSKLH KVTELAELGS 

       190        200        210        220        230        240 
DNEALLATFM IEQPGSFKTF AKLVGSMNIT EVTYRFTSER KEALVLYRVD VDEKSDLEEM 

       250        260        270        280        290        300 
IKKLNSSNMK TFNFSHNELV AEHIKHLVGG SASISDEIFG EFIFPEKAGT LSTFLEAFSP 

       310        320        330        340        350 
RWNITLCRYR DQGDINGNVL VGFQVPQSEM DEFKSQADGL GYPYELDNSN EAFNIVVAE

P31212 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools