THRC1_ARATH
ID THRC1_ARATH Reviewed; 526 AA.
AC Q9S7B5; Q39144;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Threonine synthase 1, chloroplastic;
DE EC=4.2.3.1 {ECO:0000269|PubMed:10429206};
DE AltName: Full=Protein METHIONINE OVER-ACCUMULATOR 2;
DE Flags: Precursor;
GN Name=TS1; Synonyms=MTO2; OrderedLocusNames=At4g29840; ORFNames=F27B13.80;
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 [GENOMIC DNA].
RC STRAIN=cv. Wassilewskija;
RA Bartlem D., Tamaki Y., Naito S.;
RT "Genomic nucleotide sequence of the Arabidopsis threonine synthase gene.";
RL (er) Plant Gene Register PGR99-108(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-526, AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=8706836; DOI=10.1016/0014-5793(96)00633-3;
RA Curien G., Dumas R., Ravanel S., Douce R.;
RT "Characterization of an Arabidopsis thaliana cDNA encoding an S-
RT adenosylmethionine-sensitive threonine synthase. Threonine synthase from
RT higher plants.";
RL FEBS Lett. 390:85-90(1996).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9748328; DOI=10.1021/bi980068f;
RA Curien G., Job D., Douce R., Dumas R.;
RT "Allosteric activation of Arabidopsis threonine synthase by S-
RT adenosylmethionine.";
RL Biochemistry 37:13212-13221(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBUNIT, AND CRYSTALLIZATION.
RX PubMed=10429206; DOI=10.1046/j.1432-1327.1999.00487.x;
RA Laber B., Maurer W., Hanke C., Graefe S., Ehlert S., Messerschmidt A.,
RA Clausen T.;
RT "Characterization of recombinant Arabidopsis thaliana threonine synthase.";
RL Eur. J. Biochem. 263:212-221(1999).
RN [7]
RP MUTAGENESIS OF LEU-205.
RX PubMed=10806229; DOI=10.1104/pp.123.1.101;
RA Bartlem D., Lambein I., Okamoto T., Itaya A., Uda Y., Kijima F., Tamaki Y.,
RA Nambara E., Naito S.;
RT "Mutation in the threonine synthase gene results in an over-accumulation of
RT soluble methionine in Arabidopsis.";
RL Plant Physiol. 123:101-110(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 41-526, AND PYRIDOXAL PHOSPHATE
RP AT LYS-203.
RX PubMed=11344332; DOI=10.1110/ps.44301;
RA Thomazeau K., Curien G., Dumas R., Biou V.;
RT "Crystal structure of threonine synthase from Arabidopsis thaliana.";
RL Protein Sci. 10:638-648(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 41-526 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE AND S-ADENOSYL-L-METHIONINE.
RX PubMed=16319072; DOI=10.1074/jbc.m509798200;
RA Mas-Droux C., Biou V., Dumas R.;
RT "Allosteric threonine synthase. Reorganization of the pyridoxal phosphate
RT site upon asymmetric activation through S-adenosylmethionine binding to a
RT novel site.";
RL J. Biol. Chem. 281:5188-5196(2006).
CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC phosphohomoserine and the beta-addition of water to produce L-
CC threonine. {ECO:0000269|PubMed:10429206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC Evidence={ECO:0000269|PubMed:10429206};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Allosterically activated by S-adenosyl-L-
CC methionine (SAM). Activated by S-adenosyl-L-ethionine, 5'-amino-5'-
CC deoxyadenosine, sinefungin and 5'-deoxy-5-methylthioadenosine.
CC Inhibited by AMP. {ECO:0000269|PubMed:10429206}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for O-phospho-L-homoserine (in presence of 100 uM S-
CC adenosyl-L-methionine) {ECO:0000269|PubMed:10429206};
CC KM=120 uM for O-phospho-L-homoserine (in absence of 100 uM S-
CC adenosyl-L-methionine) {ECO:0000269|PubMed:10429206};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10429206,
CC ECO:0000269|PubMed:16319072}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- DOMAIN: The N-terminal domain (1-77) is essential for regulation by S-
CC adenosyl-L-methionine and AMP, but not for dimerization.
CC -!- MISCELLANEOUS: Binds 4 S-adenosyl-L-methionine (SAM) molecules per
CC dimer. Although SAM3 and SAM4 have equivalent positions, their
CC interactions with the protein are not identical. SAM3 interacts with
CC Lys-181 and Asn-187 of monomer B, whereas SAM4 interacts only with Lys-
CC 181 of monomer A.
CC -!- MISCELLANEOUS: Much more active than TS2 at physiological
CC concentrations of S-adenosyl-L-methionine (20 uM).
CC -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR EMBL; AB027151; BAA77707.1; -; Genomic_DNA.
DR EMBL; AL050352; CAB43659.1; -; Genomic_DNA.
DR EMBL; AL161575; CAB79742.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85684.1; -; Genomic_DNA.
DR EMBL; L41666; AAB04607.1; -; mRNA.
DR PIR; T08545; T08545.
DR RefSeq; NP_194713.1; NM_119130.3.
DR PDB; 1E5X; X-ray; 2.25 A; A/B=41-526.
DR PDB; 2C2B; X-ray; 2.60 A; A/B/C/D/E/F=41-526.
DR PDB; 2C2G; X-ray; 2.61 A; A/B=41-526.
DR PDBsum; 1E5X; -.
DR PDBsum; 2C2B; -.
DR PDBsum; 2C2G; -.
DR AlphaFoldDB; Q9S7B5; -.
DR SMR; Q9S7B5; -.
DR BioGRID; 14393; 26.
DR IntAct; Q9S7B5; 1.
DR STRING; 3702.AT4G29840.1; -.
DR iPTMnet; Q9S7B5; -.
DR MetOSite; Q9S7B5; -.
DR SwissPalm; Q9S7B5; -.
DR PaxDb; Q9S7B5; -.
DR PRIDE; Q9S7B5; -.
DR ProteomicsDB; 234426; -.
DR EnsemblPlants; AT4G29840.1; AT4G29840.1; AT4G29840.
DR GeneID; 829106; -.
DR Gramene; AT4G29840.1; AT4G29840.1; AT4G29840.
DR KEGG; ath:AT4G29840; -.
DR Araport; AT4G29840; -.
DR TAIR; locus:2123939; AT4G29840.
DR eggNOG; ENOG502QSQC; Eukaryota.
DR HOGENOM; CLU_028142_5_0_1; -.
DR InParanoid; Q9S7B5; -.
DR OMA; HTLMDAV; -.
DR OrthoDB; 1361511at2759; -.
DR PhylomeDB; Q9S7B5; -.
DR BRENDA; 4.2.3.1; 399.
DR SABIO-RK; Q9S7B5; -.
DR UniPathway; UPA00050; UER00065.
DR EvolutionaryTrace; Q9S7B5; -.
DR PRO; PR:Q9S7B5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S7B5; baseline and differential.
DR Genevisible; Q9S7B5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR DisProt; DP02754; -.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00260; thrC; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis; Chloroplast;
KW Lyase; Plastid; Pyridoxal phosphate; Reference proteome;
KW S-adenosyl-L-methionine; Threonine biosynthesis; Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT CHAIN 41..526
FT /note="Threonine synthase 1, chloroplastic"
FT /id="PRO_0000033617"
FT BINDING 142..144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 165..167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:16319072"
FT BINDING 173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:16319072"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="3"
FT /note="in monomer B"
FT /evidence="ECO:0000269|PubMed:16319072"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="4"
FT /note="in monomer A"
FT /evidence="ECO:0000269|PubMed:16319072"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="3"
FT /note="in monomer B"
FT /evidence="ECO:0000269|PubMed:16319072"
FT BINDING 335..339
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT MUTAGEN 205
FT /note="L->R: In mto2-1; causes a strong decrease in the
FT concentration of soluble threonine and over-accumulation of
FT methionine."
FT /evidence="ECO:0000269|PubMed:10806229"
FT CONFLICT 2
FT /note="A -> L (in Ref. 4; AAB04607)"
FT /evidence="ECO:0000305"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1E5X"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2C2G"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:1E5X"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1E5X"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:2C2B"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 281..294
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 304..311
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:1E5X"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2C2B"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:2C2B"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:2C2B"
FT HELIX 373..378
FT /evidence="ECO:0007829|PDB:1E5X"
FT TURN 379..383
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:2C2B"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 424..436
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 443..457
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 479..486
FT /evidence="ECO:0007829|PDB:1E5X"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:1E5X"
FT HELIX 508..518
FT /evidence="ECO:0007829|PDB:1E5X"
SQ SEQUENCE 526 AA; 57777 MW; B27787A57B882AD0 CRC64;
MASSCLFNAS VSSLNPKQDP IRRHRSTSLL RHRPVVISCT ADGNNIKAPI ETAVKPPHRT
EDNIRDEARR NRSNAVNPFS AKYVPFNAAP GSTESYSLDE IVYRSRSGGL LDVEHDMEAL
KRFDGAYWRD LFDSRVGKST WPYGSGVWSK KEWVLPEIDD DDIVSAFEGN SNLFWAERFG
KQFLGMNDLW VKHCGISHTG SFKDLGMTVL VSQVNRLRKM KRPVVGVGCA STGDTSAALS
AYCASAGIPS IVFLPANKIS MAQLVQPIAN GAFVLSIDTD FDGCMKLIRE ITAELPIYLA
NSLNSLRLEG QKTAAIEILQ QFDWQVPDWV IVPGGNLGNI YAFYKGFKMC QELGLVDRIP
RMVCAQAANA NPLYLHYKSG WKDFKPMTAS TTFASAIQIG DPVSIDRAVY ALKKCNGIVE
EATEEELMDA MAQADSTGMF ICPHTGVALT ALFKLRNQGV IAPTDRTVVV STAHGLKFTQ
SKIDYHSNAI PDMACRFSNP PVDVKADFGA VMDVLKSYLG SNTLTS
