THD1_ARATH
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 03-AUG-2022, entry version 151.
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}.
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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.AT3G10050.1; -.
DR PaxDb; Q9ZSS6; -.
DR PRIDE; Q9ZSS6; -.
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; locus:2100078; AT3G10050.
DR eggNOG; KOG1250; Eukaryota.
DR HOGENOM; CLU_021152_6_2_1; -.
DR InParanoid; Q9ZSS6; -.
DR OMA; VNFPQRA; -.
DR OrthoDB; 906802at2759; -.
DR PhylomeDB; Q9ZSS6; -.
DR BioCyc; ARA:AT3G10050-MON; -.
DR SABIO-RK; Q9ZSS6; -.
DR UniPathway; UPA00047; UER00054.
DR PRO; PR:Q9ZSS6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZSS6; baseline and differential.
DR Genevisible; Q9ZSS6; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IBA:GO_Central.
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 GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.1020.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR001926; PLP-dep.
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; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 2.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR PROSITE; PS51672; ACT_LIKE; 2.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
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
