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Protein

Threonine dehydratase biosynthetic, chloroplastic

Gene

OMR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

L-threonine = 2-oxobutanoate + NH3.

Cofactori

Enzyme regulationi

Allosterically inhibited by isoleucine. Strain GM11b is isoleucine feedback insensitive and is resistant to the antimetabolite L-O-methylthreonine.

Pathway: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 2-oxobutanoate from L-threonine.
Proteins known to be involved in this subpathway in this organism are:
  1. Threonine dehydratase biosynthetic, chloroplastic (OMR1), Threonine dehydratase (At3g10050)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-oxobutanoate from L-threonine, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

  • L-threonine ammonia-lyase activity Source: TAIR
  • pyridoxal phosphate binding Source: GO_Central

GO - Biological processi

  • isoleucine biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:AT3G10050-MONOMER.
UniPathwayiUPA00047; UER00054.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine dehydratase biosynthetic, chloroplastic (EC:4.3.1.19)
Alternative name(s):
Threonine deaminase
Short name:
TD
Gene namesi
Name:OMR1
Ordered Locus Names:At3g10050
ORF Names:T22K18.12
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G10050.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi499 – 4991R → C in omr1; loss of Ile feedback sensitivity; when associated with H-544.
Mutagenesisi544 – 5441R → H in omr1; loss of Ile feedback sensitivity; when associated with C-499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 9191ChloroplastSequence AnalysisAdd
BLAST
Chaini92 – 592501Threonine dehydratase biosynthetic, chloroplasticPRO_0000033612Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei141 – 1411N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiQ9ZSS6.
PRIDEiQ9ZSS6.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G10050.1.

Structurei

3D structure databases

ProteinModelPortaliQ9ZSS6.
SMRiQ9ZSS6. Positions 48-414.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini419 – 49072ACT-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini512 – 58372ACT-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 ACT-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG1171.
HOGENOMiHOG000046975.
InParanoidiQ9ZSS6.
KOiK01754.
OMAiPQNTPSI.
PhylomeDBiQ9ZSS6.

Family and domain databases

InterProiIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01124. ilvA_2Cterm. 1 hit.
PROSITEiPS51672. ACT_LIKE. 2 hits.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ZSS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSVQLPTAQ SSLRSHIHRP SKPVVGFTHF SSRSRIAVAV LSRDETSMTP
60 70 80 90 100
PPPKLPLPRL KVSPNSLQYP AGYLGAVPER TNEAENGSIA EAMEYLTNIL
110 120 130 140 150
STKVYDIAIE SPLQLAKKLS KRLGVRMYLK REDLQPVFSF KLRGAYNMMV
160 170 180 190 200
KLPADQLAKG VICSSAGNHA QGVALSASKL GCTAVIVMPV TTPEIKWQAV
210 220 230 240 250
ENLGATVVLF GDSYDQAQAH AKIRAEEEGL TFIPPFDHPD VIAGQGTVGM
260 270 280 290 300
EITRQAKGPL HAIFVPVGGG GLIAGIAAYV KRVSPEVKII GVEPADANAM
310 320 330 340 350
ALSLHHGERV ILDQVGGFAD GVAVKEVGEE TFRISRNLMD GVVLVTRDAI
360 370 380 390 400
CASIKDMFEE KRNILEPAGA LALAGAEAYC KYYGLKDVNV VAITSGANMN
410 420 430 440 450
FDKLRIVTEL ANVGRQQEAV LATLMPEKPG SFKQFCELVG PMNISEFKYR
460 470 480 490 500
CSSEKEAVVL YSVGVHTAGE LKALQKRMES SQLKTVNLTT SDLVKDHLRY
510 520 530 540 550
LMGGRSTVGD EVLCRFTFPE RPGALMNFLD SFSPRWNITL FHYRGQGETG
560 570 580 590
ANVLVGIQVP EQEMEEFKNR AKALGYDYFL VSDDDYFKLL MH
Length:592
Mass (Da):64,635
Last modified:May 1, 1999 - v1
Checksum:i16658747052FAE7C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT51712.
RefSeqiNP_187616.1. NM_111840.2.
UniGeneiAt.10929.

Genome annotation databases

EnsemblPlantsiAT3G10050.1; AT3G10050.1; AT3G10050.
GeneIDi820166.
KEGGiath:AT3G10050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT51712.
RefSeqiNP_187616.1. NM_111840.2.
UniGeneiAt.10929.

3D structure databases

ProteinModelPortaliQ9ZSS6.
SMRiQ9ZSS6. Positions 48-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G10050.1.

Proteomic databases

PaxDbiQ9ZSS6.
PRIDEiQ9ZSS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G10050.1; AT3G10050.1; AT3G10050.
GeneIDi820166.
KEGGiath:AT3G10050.

Organism-specific databases

TAIRiAT3G10050.

Phylogenomic databases

eggNOGiCOG1171.
HOGENOMiHOG000046975.
InParanoidiQ9ZSS6.
KOiK01754.
OMAiPQNTPSI.
PhylomeDBiQ9ZSS6.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00054.
BioCyciARA:AT3G10050-MONOMER.

Miscellaneous databases

PROiQ9ZSS6.

Family and domain databases

InterProiIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01124. ilvA_2Cterm. 1 hit.
PROSITEiPS51672. ACT_LIKE. 2 hits.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTHD1_ARATH
AccessioniPrimary (citable) accession number: Q9ZSS6
Secondary accession number(s): Q9SPF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 1999
Last modified: June 24, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.