THA2_ARATH
ID THA2_ARATH Reviewed; 355 AA.
AC Q9FPH3; Q9M835;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable low-specificity L-threonine aldolase 2;
DE EC=4.1.2.48 {ECO:0000269|PubMed:17172352};
DE AltName: Full=Threonine aldolase 2;
GN Name=THA2; OrderedLocusNames=At3g04520; ORFNames=T27C4.17;
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=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 [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].
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].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
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: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:17172352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19626;
CC Evidence={ECO:0000305|PubMed:17172352};
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:17172352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26210;
CC Evidence={ECO:0000305|PubMed:17172352};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.8 mM for L-threonine {ECO:0000269|PubMed:17172352};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via aldolase
CC pathway; acetaldehyde and glycine from L-threonine: step 1/1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FPH3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf vasculature and flowers.
CC {ECO:0000269|PubMed:17172352}.
CC -!- DISRUPTION PHENOTYPE: Lethal albino phenotype when homozygous.
CC {ECO:0000269|PubMed:17172352}.
CC -!- SIMILARITY: Belongs to the threonine aldolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63783.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022287; AAF63783.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74091.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65683.1; -; Genomic_DNA.
DR EMBL; AF325033; AAG40385.1; -; mRNA.
DR EMBL; AY091093; AAM14044.1; -; mRNA.
DR EMBL; AY123033; AAM67566.1; -; mRNA.
DR EMBL; AK175345; BAD43108.1; -; mRNA.
DR EMBL; AY085456; AAM62682.1; -; mRNA.
DR RefSeq; NP_001327633.1; NM_001337534.1. [Q9FPH3-1]
DR RefSeq; NP_566228.1; NM_111323.4. [Q9FPH3-1]
DR AlphaFoldDB; Q9FPH3; -.
DR SMR; Q9FPH3; -.
DR STRING; 3702.AT3G04520.1; -.
DR PaxDb; Q9FPH3; -.
DR PRIDE; Q9FPH3; -.
DR ProteomicsDB; 234386; -. [Q9FPH3-1]
DR EnsemblPlants; AT3G04520.1; AT3G04520.1; AT3G04520. [Q9FPH3-1]
DR EnsemblPlants; AT3G04520.3; AT3G04520.3; AT3G04520. [Q9FPH3-1]
DR GeneID; 819608; -.
DR Gramene; AT3G04520.1; AT3G04520.1; AT3G04520. [Q9FPH3-1]
DR Gramene; AT3G04520.3; AT3G04520.3; AT3G04520. [Q9FPH3-1]
DR KEGG; ath:AT3G04520; -.
DR Araport; AT3G04520; -.
DR TAIR; locus:2100860; AT3G04520.
DR eggNOG; KOG1368; Eukaryota.
DR InParanoid; Q9FPH3; -.
DR OMA; ENTHNVC; -.
DR OrthoDB; 1099858at2759; -.
DR PhylomeDB; Q9FPH3; -.
DR SABIO-RK; Q9FPH3; -.
DR UniPathway; UPA00044; UER00429.
DR PRO; PR:Q9FPH3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FPH3; baseline and differential.
DR Genevisible; Q9FPH3; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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..355
FT /note="Probable low-specificity L-threonine aldolase 2"
FT /id="PRO_0000428660"
FT MOD_RES 211
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 38252 MW; D7D1EFDBA18B517E CRC64;
MVTPTTIRTV DLRSDTVTKP TESMRSAMAN AEVDDDVLGN DPTALRLEKE VAEIAGKEAA
MFVPSGTMGN LISVLVHCDE RGSEVILGDD SHIHIYENGG VSSLGGVHPR TVKNEEDGTM
EIGAIEAAVR SPKGDLHHPV TKLICLENTQ ANCGGRCLPI EYIDKVGELA KKHGLKLHID
GARIFNASVA LGVPVKRIVQ AADSVSICLS KGIGAPVGSV IVGSKKFITK ARWLRKTLGG
GMRQIGVLCA AALVALHENV AKLEDDHKKA RVLAEGLNRI ERLRVNVAAV ETNIIYVDIP
EDPKFGAEEA CKSLEDVGVL VIPQATFRIR IVLHHQISDV DVEYVLSCFE KIFHS
