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Q9ZSS6

- THD1_ARATH

UniProt

Q9ZSS6 - THD1_ARATH

Protein

Threonine dehydratase biosynthetic, chloroplastic

Gene

OMR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    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

    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

    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.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9ZSS6.
    GenevestigatoriQ9ZSS6.

    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.
    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

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    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

    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: October 1, 2014
    This is version 108 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