THA1_ARATH
ID THA1_ARATH Reviewed; 358 AA.
AC Q8RXU4; B9DG61; Q2V4P5; Q8LC88; Q9FRS2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Low-specificity L-threonine aldolase 1 {ECO:0000303|PubMed:15255874, ECO:0000303|PubMed:17172352};
DE EC=4.1.2.48 {ECO:0000269|PubMed:15255874};
DE AltName: Full=Threonine aldolase 1 {ECO:0000303|PubMed:15255874, ECO:0000303|PubMed:17172352};
GN Name=THA1 {ECO:0000303|PubMed:15255874, ECO:0000303|PubMed:17172352};
GN OrderedLocusNames=At1g08630 {ECO:0000312|Araport:AT1G08630};
GN ORFNames=F22O13.11 {ECO:0000312|EMBL:AAF99780.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, PATHWAY, AND
RP MUTAGENESIS OF GLY-114.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=15255874; DOI=10.1111/j.1365-313x.2004.02140.x;
RA Jander G., Norris S.R., Joshi V., Fraga M., Rugg A., Yu S., Li L.,
RA Last R.L.;
RT "Application of a high-throughput HPLC-MS/MS assay to Arabidopsis mutant
RT screening; evidence that threonine aldolase plays a role in seed
RT nutritional quality.";
RL Plant J. 39:465-475(2004).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-114.
RC STRAIN=cv. Columbia;
RX PubMed=17172352; DOI=10.1105/tpc.106.044958;
RA Joshi V., Laubengayer K.M., Schauer N., Fernie A.R., Jander G.;
RT "Two Arabidopsis threonine aldolases are nonredundant and compete with
RT threonine deaminase for a common substrate pool.";
RL Plant Cell 18:3564-3575(2006).
CC -!- FUNCTION: Threonine aldolase involved in threonine degradation to
CC glycine. May play a role in the removal of L-allo-threonine.
CC {ECO:0000269|PubMed:15255874, ECO:0000269|PubMed:17172352}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:19625,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57926; EC=4.1.2.48;
CC Evidence={ECO:0000269|PubMed:15255874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19626;
CC Evidence={ECO:0000269|PubMed:15255874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-allo-threonine = acetaldehyde + glycine;
CC Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:58585; EC=4.1.2.48;
CC Evidence={ECO:0000269|PubMed:15255874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26210;
CC Evidence={ECO:0000269|PubMed:15255874};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:O07051};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 mM for L-threonine {ECO:0000269|PubMed:15255874};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via aldolase
CC pathway; acetaldehyde and glycine from L-threonine: step 1/1.
CC {ECO:0000269|PubMed:15255874}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RXU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RXU4-2; Sequence=VSP_054082;
CC -!- TISSUE SPECIFICITY: Expressed in root tips, seedlings, carpels and
CC seeds. {ECO:0000269|PubMed:17172352}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have 50-fold increase in seed Thr content
CC and 2-fold decrease in seedling Gly content.
CC {ECO:0000269|PubMed:17172352}.
CC -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003981; AAF99780.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28320.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28321.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28322.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28323.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28324.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59683.1; -; Genomic_DNA.
DR EMBL; AY080670; AAL86346.1; -; mRNA.
DR EMBL; AY117227; AAM51302.1; -; mRNA.
DR EMBL; AK317034; BAH19728.1; -; mRNA.
DR EMBL; AK230078; BAF01898.1; -; mRNA.
DR EMBL; AY086734; AAM63785.1; -; mRNA.
DR PIR; T00716; T00716.
DR RefSeq; NP_001031001.2; NM_001035924.2. [Q8RXU4-1]
DR RefSeq; NP_001077492.1; NM_001084023.1. [Q8RXU4-2]
DR RefSeq; NP_001318956.1; NM_001331780.1. [Q8RXU4-1]
DR RefSeq; NP_563822.1; NM_100736.3. [Q8RXU4-1]
DR RefSeq; NP_849614.1; NM_179283.2. [Q8RXU4-1]
DR RefSeq; NP_849615.1; NM_179284.4. [Q8RXU4-1]
DR AlphaFoldDB; Q8RXU4; -.
DR SMR; Q8RXU4; -.
DR STRING; 3702.AT1G08630.1; -.
DR PaxDb; Q8RXU4; -.
DR PRIDE; Q8RXU4; -.
DR ProteomicsDB; 234327; -. [Q8RXU4-1]
DR EnsemblPlants; AT1G08630.1; AT1G08630.1; AT1G08630. [Q8RXU4-1]
DR EnsemblPlants; AT1G08630.2; AT1G08630.2; AT1G08630. [Q8RXU4-1]
DR EnsemblPlants; AT1G08630.3; AT1G08630.3; AT1G08630. [Q8RXU4-1]
DR EnsemblPlants; AT1G08630.4; AT1G08630.4; AT1G08630. [Q8RXU4-1]
DR EnsemblPlants; AT1G08630.5; AT1G08630.5; AT1G08630. [Q8RXU4-2]
DR EnsemblPlants; AT1G08630.6; AT1G08630.6; AT1G08630. [Q8RXU4-1]
DR GeneID; 837385; -.
DR Gramene; AT1G08630.1; AT1G08630.1; AT1G08630. [Q8RXU4-1]
DR Gramene; AT1G08630.2; AT1G08630.2; AT1G08630. [Q8RXU4-1]
DR Gramene; AT1G08630.3; AT1G08630.3; AT1G08630. [Q8RXU4-1]
DR Gramene; AT1G08630.4; AT1G08630.4; AT1G08630. [Q8RXU4-1]
DR Gramene; AT1G08630.5; AT1G08630.5; AT1G08630. [Q8RXU4-2]
DR Gramene; AT1G08630.6; AT1G08630.6; AT1G08630. [Q8RXU4-1]
DR KEGG; ath:AT1G08630; -.
DR Araport; AT1G08630; -.
DR TAIR; locus:2025645; AT1G08630.
DR eggNOG; KOG1368; Eukaryota.
DR InParanoid; Q8RXU4; -.
DR OMA; NKGGGAC; -.
DR OrthoDB; 1099858at2759; -.
DR PhylomeDB; Q8RXU4; -.
DR SABIO-RK; Q8RXU4; -.
DR UniPathway; UPA00044; UER00429.
DR PRO; PR:Q8RXU4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RXU4; baseline and differential.
DR Genevisible; Q8RXU4; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008732; F:L-allo-threonine aldolase activity; IBA:GO_Central.
DR GO; GO:0004793; F:threonine aldolase activity; IDA:TAIR.
DR GO; GO:0006545; P:glycine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006567; P:threonine catabolic process; IMP:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR023603; Low_specificity_L-TA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..358
FT /note="Low-specificity L-threonine aldolase 1"
FT /id="PRO_0000428659"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O07051"
FT VAR_SEQ 270..283
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_054082"
FT MUTAGEN 114
FT /note="G->R: In tha1-1; loss of function; 50-fold increase
FT in seed Thr content and 2-fold decrease in seedling Gly
FT content."
FT /evidence="ECO:0000269|PubMed:15255874,
FT ECO:0000269|PubMed:17172352"
FT CONFLICT 321
FT /note="N -> K (in Ref. 6; AAM63785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38942 MW; E38254B11A967514 CRC64;
MVMRSVDLRS DTVTRPTDAM REAMCNAEVD DDVLGYDPTA RRLEEEMAKM MGKEAALFVP
SGTMGNLISV MVHCDVRGSE VILGDNCHIH VYENGGISTI GGVHPKTVKN EEDGTMDLEA
IEAAIRDPKG STFYPSTRLI CLENTHANSG GRCLSVEYTE KVGEIAKRHG VKLHIDGARL
FNASIALGVP VHKLVKAADS VQVCLSKGLG APVGSVIVGS QSFIEKAKTV RKTLGGGMRQ
IGVLCAAALV ALQENLPKLQ HDHKKAKLLA EGLNQMKGIR VNVAAVETNM IFMDMEDGSR
LTAEKLRKNL EENGILLIRG NSSRIRIVIH HQITTSDVHY TLSCFQQAML TMQEPSRT
