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Q9ZSS6 (THD1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Plastidchloroplast By similarity.

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Contains 2 ACT-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 9191Chloroplast Potential
Chain92 – 592501Threonine dehydratase biosynthetic, chloroplastic
PRO_0000033612

Regions

Domain419 – 49072ACT-like 1
Domain512 – 58372ACT-like 2

Amino acid modifications

Modified residue1411N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Mutagenesis4991R → C in omr1; loss of Ile feedback sensitivity; when associated with H-544.
Mutagenesis5441R → H in omr1; loss of Ile feedback sensitivity; when associated with C-499.

Sequences

Sequence LengthMass (Da)Tools
Q9ZSS6 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 16658747052FAE7C

FASTA59264,635
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRT51712.
RefSeqNP_187616.1. NM_111840.2.
UniGeneAt.10929.

3D structure databases

ProteinModelPortalQ9ZSS6.
SMRQ9ZSS6. Positions 48-414.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9ZSS6.
PRIDEQ9ZSS6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G10050.1; AT3G10050.1; AT3G10050.
GeneID820166.
KEGGath:AT3G10050.

Organism-specific databases

TAIRAT3G10050.

Phylogenomic databases

eggNOGCOG1171.
HOGENOMHOG000046975.
InParanoidQ9ZSS6.
KOK01754.
OMAGMKKYIQ.
PhylomeDBQ9ZSS6.

Enzyme and pathway databases

BioCycARA:AT3G10050-MONOMER.
UniPathwayUPA00047; UER00054.

Gene expression databases

ArrayExpressQ9ZSS6.
GenevestigatorQ9ZSS6.

Family and domain databases

InterProIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR01124. ilvA_2Cterm. 1 hit.
PROSITEPS51672. ACT_LIKE. 2 hits.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9ZSS6.

Entry information

Entry nameTHD1_ARATH
AccessionPrimary (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: June 11, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names