ID   THD1_ARATH              Reviewed;         592 AA.
AC   Q9ZSS6; Q9SPF1;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Threonine dehydratase biosynthetic, chloroplastic;
DE            EC=4.3.1.19;
DE   AltName: Full=Threonine deaminase;
DE            Short=TD;
DE   Flags: Precursor;
GN   Name=OMR1; OrderedLocusNames=At3g10050; ORFNames=T22K18.12;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Mourad G., Emerick R., Marion A., Smith A.;
RT   "Cloning and sequencing of a cDNA encoding threonine dehydratase/ deaminase
RT   of Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR98-199(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mourad G.S., Smith A.M.;
RT   "Molecular characterization of the genomic clone, including the promoter
RT   sequences, of threonine dehydratase/deaminase from Arabidopsis thaliana.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MUTANT OMR1.
RC   STRAIN=cv. Columbia;
RA   Mourad G., Emerick R., Smith A.;
RT   "Molecular cloning and sequencing of a cDNA encoding an isoleucine feedback
RT   insensitive threonine dehydratase/deaminase of Arabidopsis thaliana line
RT   GM11b.";
RL   (er) Plant Gene Register PGR00-020(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Catalyzes the formation of alpha-ketobutyrate from threonine
CC       in a two-step reaction. The first step is a dehydration of threonine,
CC       followed by rehydration and liberation of ammonia.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Allosterically inhibited by isoleucine. Strain
CC       GM11b is isoleucine feedback insensitive and is resistant to the
CC       antimetabolite L-O-methylthreonine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF096281; AAC97936.1; -; mRNA.
DR   EMBL; AF221984; AAF32370.1; -; Genomic_DNA.
DR   EMBL; AF177212; AAD54324.1; -; mRNA.
DR   EMBL; AC010927; AAF04418.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74854.1; -; Genomic_DNA.
DR   EMBL; AY065037; AAL57674.1; -; mRNA.
DR   PIR; T51712; T51712.
DR   RefSeq; NP_187616.1; NM_111840.3.
DR   AlphaFoldDB; Q9ZSS6; -.
DR   SMR; Q9ZSS6; -.
DR   STRING; 3702.Q9ZSS6; -.
DR   PaxDb; 3702-AT3G10050-1; -.
DR   ProteomicsDB; 234328; -.
DR   EnsemblPlants; AT3G10050.1; AT3G10050.1; AT3G10050.
DR   GeneID; 820166; -.
DR   Gramene; AT3G10050.1; AT3G10050.1; AT3G10050.
DR   KEGG; ath:AT3G10050; -.
DR   Araport; AT3G10050; -.
DR   TAIR; AT3G10050; OMR1.
DR   eggNOG; KOG1250; Eukaryota.
DR   HOGENOM; CLU_021152_6_2_1; -.
DR   InParanoid; Q9ZSS6; -.
DR   OMA; TRFEYTK; -.
DR   OrthoDB; 5476420at2759; -.
DR   PhylomeDB; Q9ZSS6; -.
DR   BioCyc; ARA:AT3G10050-MONOMER; -.
DR   SABIO-RK; Q9ZSS6; -.
DR   UniPathway; UPA00047; UER00054.
DR   PRO; PR:Q9ZSS6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9ZSS6; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:TAIR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IMP:TAIR.
DR   CDD; cd04906; ACT_ThrD-I_1; 1.
DR   CDD; cd04907; ACT_ThrD-I_2; 1.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001721; TD_ACT-like.
DR   InterPro; IPR038110; TD_ACT-like_sf.
DR   InterPro; IPR005787; Thr_deHydtase_biosynth.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01124; ilvA_2Cterm; 1.
DR   PANTHER; PTHR48078:SF11; THREONINE DEHYDRATASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 2.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51672; ACT_LIKE; 2.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
DR   Genevisible; Q9ZSS6; AT.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Chloroplast;
KW   Isoleucine biosynthesis; Lyase; Plastid; Pyridoxal phosphate;
KW   Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..91
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           92..592
FT                   /note="Threonine dehydratase biosynthetic, chloroplastic"
FT                   /id="PRO_0000033612"
FT   DOMAIN          419..490
FT                   /note="ACT-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   DOMAIN          512..583
FT                   /note="ACT-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01008"
FT   MOD_RES         141
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         499
FT                   /note="R->C: In omr1; loss of Ile feedback sensitivity;
FT                   when associated with H-544."
FT   MUTAGEN         544
FT                   /note="R->H: In omr1; loss of Ile feedback sensitivity;
FT                   when associated with C-499."
SQ   SEQUENCE   592 AA;  64635 MW;  16658747052FAE7C CRC64;
     MNSVQLPTAQ SSLRSHIHRP SKPVVGFTHF SSRSRIAVAV LSRDETSMTP PPPKLPLPRL
     KVSPNSLQYP AGYLGAVPER TNEAENGSIA EAMEYLTNIL STKVYDIAIE SPLQLAKKLS
     KRLGVRMYLK REDLQPVFSF KLRGAYNMMV KLPADQLAKG VICSSAGNHA QGVALSASKL
     GCTAVIVMPV TTPEIKWQAV ENLGATVVLF GDSYDQAQAH AKIRAEEEGL TFIPPFDHPD
     VIAGQGTVGM EITRQAKGPL HAIFVPVGGG GLIAGIAAYV KRVSPEVKII GVEPADANAM
     ALSLHHGERV ILDQVGGFAD GVAVKEVGEE TFRISRNLMD GVVLVTRDAI CASIKDMFEE
     KRNILEPAGA LALAGAEAYC KYYGLKDVNV VAITSGANMN FDKLRIVTEL ANVGRQQEAV
     LATLMPEKPG SFKQFCELVG PMNISEFKYR CSSEKEAVVL YSVGVHTAGE LKALQKRMES
     SQLKTVNLTT SDLVKDHLRY LMGGRSTVGD EVLCRFTFPE RPGALMNFLD SFSPRWNITL
     FHYRGQGETG ANVLVGIQVP EQEMEEFKNR AKALGYDYFL VSDDDYFKLL MH
//