Q9ZSS6 (THD1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Threonine dehydratase biosynthetic, chloroplastic
EC=4.3.1.19

Alternative name(s):
Threonine deaminase
Short name=TD

Gene names

Name:	OMR1
Ordered Locus Names:	At3g10050
ORF Names:	T22K18.12

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of alpha-ketobutyrate from threonine in a two-step reaction. The first step is a dehydration of threonine, followed by rehydration and liberation of ammonia.
Catalytic activity	L-threonine = 2-oxobutanoate + NH3.
Cofactor	Pyridoxal phosphate By similarity.
Enzyme regulation	Allosterically inhibited by isoleucine. Strain GM11b is isoleucine feedback insensitive and is resistant to the antimetabolite L-O-methylthreonine.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
Subcellular location	Plastid › chloroplast By similarity.
Sequence similarities	Belongs to the serine/threonine dehydratase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	isoleucine biosynthetic process Traceable author statement PubMed 12228340. Source: TAIR
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	L-threonine ammonia-lyase activity Inferred from mutant phenotype PubMed 12228340. Source: TAIR 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
	Transit peptide	1 – 91	91	Chloroplast Potential
	Chain	92 – 592	501	Threonine dehydratase biosynthetic, chloroplastic		PRO_0000033612
Amino acid modifications
	Modified residue	141	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Mutagenesis	499	1	R → C in omr1; loss of Ile feedback sensitivity; when associated with H-544.
	Mutagenesis	544	1	R → H in omr1; loss of Ile feedback sensitivity; when associated with C-499.

Sequences

	Sequence		Length	Mass (Da)
	Q9ZSS6 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 16658747052FAE7C	FASTA	592	64,635
	10 20 30 40 50 60 MNSVQLPTAQ SSLRSHIHRP SKPVVGFTHF SSRSRIAVAV LSRDETSMTP PPPKLPLPRL 70 80 90 100 110 120 KVSPNSLQYP AGYLGAVPER TNEAENGSIA EAMEYLTNIL STKVYDIAIE SPLQLAKKLS 130 140 150 160 170 180 KRLGVRMYLK REDLQPVFSF KLRGAYNMMV KLPADQLAKG VICSSAGNHA QGVALSASKL 190 200 210 220 230 240 GCTAVIVMPV TTPEIKWQAV ENLGATVVLF GDSYDQAQAH AKIRAEEEGL TFIPPFDHPD 250 260 270 280 290 300 VIAGQGTVGM EITRQAKGPL HAIFVPVGGG GLIAGIAAYV KRVSPEVKII GVEPADANAM 310 320 330 340 350 360 ALSLHHGERV ILDQVGGFAD GVAVKEVGEE TFRISRNLMD GVVLVTRDAI CASIKDMFEE 370 380 390 400 410 420 KRNILEPAGA LALAGAEAYC KYYGLKDVNV VAITSGANMN FDKLRIVTEL ANVGRQQEAV 430 440 450 460 470 480 LATLMPEKPG SFKQFCELVG PMNISEFKYR CSSEKEAVVL YSVGVHTAGE LKALQKRMES 490 500 510 520 530 540 SQLKTVNLTT SDLVKDHLRY LMGGRSTVGD EVLCRFTFPE RPGALMNFLD SFSPRWNITL 550 560 570 580 590 FHYRGQGETG ANVLVGIQVP EQEMEEFKNR AKALGYDYFL VSDDDYFKLL MH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a cDNA encoding threonine dehydratase/ deaminase of Arabidopsis thaliana." Mourad G., Emerick R., Marion A., Smith A. Plant Gene Register PGR98-199 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Molecular characterization of the genomic clone, including the promoter sequences, of threonine dehydratase/deaminase from Arabidopsis thaliana." Mourad G.S., Smith A.M. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Molecular cloning and sequencing of a cDNA encoding an isoleucine feedback insensitive threonine dehydratase/deaminase of Arabidopsis thaliana line GM11b." Mourad G., Emerick R., Smith A. Plant Gene Register PGR00-020 Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTANT OMR1. Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF096281 mRNA. Translation: AAC97936.1. AF221984 Genomic DNA. Translation: AAF32370.1. AF177212 mRNA. Translation: AAD54324.1. AC010927 Genomic DNA. Translation: AAF04418.1. CP002686 Genomic DNA. Translation: AEE74854.1. AY065037 mRNA. Translation: AAL57674.1.
IPI	IPI00523919.
PIR	T51712.
RefSeq	NP_187616.1. NM_111840.2.
UniGene	At.10929.
3D structure databases
ProteinModelPortal	Q9ZSS6.
SMR	Q9ZSS6. Positions 48-414.
ModBase	Search...
Proteomic databases
PaxDb	Q9ZSS6.
PRIDE	Q9ZSS6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G10050.1; AT3G10050.1; AT3G10050.
GeneID	820166.
KEGG	ath:AT3G10050.
Organism-specific databases
TAIR	At3g10050.
Phylogenomic databases
eggNOG	COG1171.
HOGENOM	HOG000046975.
InParanoid	Q9ZSS6.
KO	K01754.
OMA	AAYYKAV.
PhylomeDB	Q9ZSS6.
ProtClustDB	PLN02550.
Enzyme and pathway databases
UniPathway	UPA00047; UER00054.
Gene expression databases
ArrayExpress	Q9ZSS6.
Genevestigator	Q9ZSS6.
GermOnline	AT3G10050. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR005787. Thr_deHydtase_biosynth. IPR001721. Thr_deHydtase_C_reg_dom. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view]
Pfam	PF00291. PALP. 1 hit. PF00585. Thr_dehydrat_C. 2 hits. [Graphical view]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR01124. ilvA_2Cterm. 1 hit.
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THD1_ARATH

Accession

Primary (citable) accession number: Q9ZSS6
Secondary accession number(s): Q9SPF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program