Reviewed, UniProtKB/Swiss-Prot P31212 (THD1_SOLTU)

Names and origin

Protein names

Recommended name:
    Threonine dehydratase biosynthetic
    EC=4.3.1.19
Alternative name(s):
    Threonine deaminase
      Short name=TD

Gene names

Name:

TD

Organism

Solanum tuberosum (Potato)

Taxonomic identifier

4113 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	359 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (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 structure	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.
Sequence similarities	Belongs to the serine/threonine dehydratase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis Stress response
Cellular component	Chloroplast Plastid
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-threonine ammonia-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 359	›359	Threonine dehydratase biosynthetic		PRO_0000185581
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P31212-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 94DC75974AF9EA30	FASTA	359	39,088
	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

References

[1]

"General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding." Hildmann T., Ebneth M., Pena-Cortes H., Sanchez-Serrano J.J., Willmitzer L., Prat S. Plant Cell 4:1157-1170(1992) [PubMed: 1392612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Desiree. Tissue: Leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X67846 mRNA. Translation: CAA48039.1.
PIR	PQ0468.
3D structure databases
HSSP	HSSP built from PDB template 1TDJ based on UniProtKB P04968.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.3.1.19. 296.
Family and domain databases
InterPro	IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR001721. Thr_deHydtase_C. [Graphical view]
Pfam	PF00291. PALP. 1 hit. PF00585. Thr_dehydrat_C. 2 hits. [Graphical view]
PROSITE	PS00165. DEHYDRATASE_SER_THR. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THD1_SOLTU

Accession

Primary (citable) accession number: P31212

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)