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Q9ZSS6

- THD1_ARATH

UniProt

Q9ZSS6 - THD1_ARATH

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Protein

Threonine dehydratase biosynthetic, chloroplastic

Gene
OMR1, At3g10050, T22K18.12
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Pyridoxal phosphate By similarity.

Enzyme regulationi

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

Pathwayi

GO - Molecular functioni

  1. L-threonine ammonia-lyase activity Source: TAIR
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. 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: Chromosome 3

Organism-specific databases

TAIRiAT3G10050.

Subcellular locationi

Plastidchloroplast By similarity

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
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 – 9191Chloroplast Reviewed predictionAdd
BLAST
Chaini92 – 592501Threonine dehydratase biosynthetic, chloroplasticPRO_0000033612Add
BLAST

Amino acid modifications

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

Proteomic databases

PaxDbiQ9ZSS6.
PRIDEiQ9ZSS6.

Expressioni

Gene expression databases

ArrayExpressiQ9ZSS6.
GenevestigatoriQ9ZSS6.

Structurei

3D structure databases

ProteinModelPortaliQ9ZSS6.
SMRiQ9ZSS6. Positions 48-414.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 ACT-like domains.

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG1171.
HOGENOMiHOG000046975.
InParanoidiQ9ZSS6.
KOiK01754.
OMAiGMKKYIQ.
PhylomeDBiQ9ZSS6.

Family and domain databases

InterProiIPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[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

MNSVQLPTAQ SSLRSHIHRP SKPVVGFTHF SSRSRIAVAV LSRDETSMTP    50
PPPKLPLPRL KVSPNSLQYP AGYLGAVPER TNEAENGSIA EAMEYLTNIL 100
STKVYDIAIE SPLQLAKKLS KRLGVRMYLK REDLQPVFSF KLRGAYNMMV 150
KLPADQLAKG VICSSAGNHA QGVALSASKL GCTAVIVMPV TTPEIKWQAV 200
ENLGATVVLF GDSYDQAQAH AKIRAEEEGL TFIPPFDHPD VIAGQGTVGM 250
EITRQAKGPL HAIFVPVGGG GLIAGIAAYV KRVSPEVKII GVEPADANAM 300
ALSLHHGERV ILDQVGGFAD GVAVKEVGEE TFRISRNLMD GVVLVTRDAI 350
CASIKDMFEE KRNILEPAGA LALAGAEAYC KYYGLKDVNV VAITSGANMN 400
FDKLRIVTEL ANVGRQQEAV LATLMPEKPG SFKQFCELVG PMNISEFKYR 450
CSSEKEAVVL YSVGVHTAGE LKALQKRMES SQLKTVNLTT SDLVKDHLRY 500
LMGGRSTVGD EVLCRFTFPE RPGALMNFLD SFSPRWNITL FHYRGQGETG 550
ANVLVGIQVP EQEMEEFKNR AKALGYDYFL VSDDDYFKLL MH 592
Length:592
Mass (Da):64,635
Last modified:May 1, 1999 - v1
Checksum:i16658747052FAE7C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi T51712.
RefSeqi NP_187616.1. NM_111840.2.
UniGenei At.10929.

3D structure databases

ProteinModelPortali Q9ZSS6.
SMRi Q9ZSS6. Positions 48-414.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9ZSS6.
PRIDEi Q9ZSS6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G10050.1 ; AT3G10050.1 ; AT3G10050 .
GeneIDi 820166.
KEGGi ath:AT3G10050.

Organism-specific databases

TAIRi AT3G10050.

Phylogenomic databases

eggNOGi COG1171.
HOGENOMi HOG000046975.
InParanoidi Q9ZSS6.
KOi K01754.
OMAi GMKKYIQ.
PhylomeDBi Q9ZSS6.

Enzyme and pathway databases

UniPathwayi UPA00047 ; UER00054 .
BioCyci ARA:AT3G10050-MONOMER.

Miscellaneous databases

PROi Q9ZSS6.

Gene expression databases

ArrayExpressi Q9ZSS6.
Genevestigatori Q9ZSS6.

Family and domain databases

InterProi IPR001721. ACT-like_dom.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR005787. Thr_deHydtase_biosynth.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 2 hits.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR01124. ilvA_2Cterm. 1 hit.
PROSITEi PS51672. ACT_LIKE. 2 hits.
PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 11, 2014
This is version 107 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

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