TAR1_ARATH
ID TAR1_ARATH Reviewed; 388 AA.
AC Q9LR29; F4I655;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Tryptophan aminotransferase-related protein 1;
DE EC=2.6.1.27;
DE EC=2.6.1.99;
GN Name=TAR1; OrderedLocusNames=At1g23320; ORFNames=F26F24.17;
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=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 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY ETHYLENE,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18394997; DOI=10.1016/j.cell.2008.01.047;
RA Stepanova A.N., Robertson-Hoyt J., Yun J., Benavente L.M., Xie D.Y.,
RA Dolezal K., Schlereth A., Juergens G., Alonso J.M.;
RT "TAA1-mediated auxin biosynthesis is essential for hormone crosstalk and
RT plant development.";
RL Cell 133:177-191(2008).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18394996; DOI=10.1016/j.cell.2008.01.049;
RA Tao Y., Ferrer J.L., Ljung K., Pojer F., Hong F., Long J.A., Li L.,
RA Moreno J.E., Bowman M.E., Ivans L.J., Cheng Y., Lim J., Zhao Y.,
RA Ballare C.L., Sandberg G., Noel J.P., Chory J.;
RT "Rapid synthesis of auxin via a new tryptophan-dependent pathway is
RT required for shade avoidance in plants.";
RL Cell 133:164-176(2008).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=22108404; DOI=10.1105/tpc.111.089029;
RA He W., Brumos J., Li H., Ji Y., Ke M., Gong X., Zeng Q., Li W., Zhang X.,
RA An F., Wen X., Li P., Chu J., Sun X., Yan C., Yan N., Xie D.Y., Raikhel N.,
RA Yang Z., Stepanova A.N., Alonso J.M., Guo H.;
RT "A small-molecule screen identifies L-kynurenine as a competitive inhibitor
RT of TAA1/TAR activity in ethylene-directed auxin biosynthesis and root
RT growth in Arabidopsis.";
RL Plant Cell 23:3944-3960(2011).
CC -!- FUNCTION: Probably involved in auxin production. TAA1, TAR1 and TAR2
CC are required for proper embryo patterning.
CC {ECO:0000269|PubMed:18394997}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-tryptophan = indole-3-pyruvate + L-
CC glutamate; Xref=Rhea:RHEA:14093, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:29985, ChEBI:CHEBI:57912; EC=2.6.1.27;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine;
CC Xref=Rhea:RHEA:27586, ChEBI:CHEBI:15361, ChEBI:CHEBI:17640,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:57972; EC=2.6.1.99;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q9S7N2};
CC -!- ACTIVITY REGULATION: Inhibited by L-kynurenine.
CC {ECO:0000269|PubMed:22108404}.
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Very low expression in seedlings.
CC {ECO:0000269|PubMed:18394997}.
CC -!- INDUCTION: Slightly up-regulated by ethylene.
CC {ECO:0000269|PubMed:18394997}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:18394997}.
CC -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87014.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AC005292; AAF87014.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE30372.1; -; Genomic_DNA.
DR RefSeq; NP_173746.1; NM_102181.1.
DR AlphaFoldDB; Q9LR29; -.
DR SMR; Q9LR29; -.
DR BioGRID; 24180; 1.
DR STRING; 3702.AT1G23320.1; -.
DR PaxDb; Q9LR29; -.
DR PRIDE; Q9LR29; -.
DR ProteomicsDB; 234219; -.
DR EnsemblPlants; AT1G23320.1; AT1G23320.1; AT1G23320.
DR GeneID; 838941; -.
DR Gramene; AT1G23320.1; AT1G23320.1; AT1G23320.
DR KEGG; ath:AT1G23320; -.
DR Araport; AT1G23320; -.
DR TAIR; locus:2028010; AT1G23320.
DR eggNOG; ENOG502QTGD; Eukaryota.
DR HOGENOM; CLU_036760_1_0_1; -.
DR InParanoid; Q9LR29; -.
DR OMA; IVPAYPA; -.
DR OrthoDB; 544719at2759; -.
DR BRENDA; 2.6.1.27; 399.
DR UniPathway; UPA00151; -.
DR PRO; PR:Q9LR29; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LR29; baseline and differential.
DR Genevisible; Q9LR29; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0050362; F:L-tryptophan:2-oxoglutarate aminotransferase activity; ISS:TAIR.
DR GO; GO:0080097; F:L-tryptophan:pyruvate aminotransferase activity; ISS:TAIR.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0048825; P:cotyledon development; IGI:TAIR.
DR GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IGI:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0080022; P:primary root development; IGI:TAIR.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR Gene3D; 2.10.25.30; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR006948; Alliinase_C.
DR InterPro; IPR037029; Alliinase_N_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF04864; Alliinase_C; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Auxin biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..388
FT /note="Tryptophan aminotransferase-related protein 1"
FT /id="PRO_0000411674"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 101..102
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 169
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 190..193
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 213..216
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 224
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 388 AA; 44064 MW; 4B5FEA35566BBD12 CRC64;
MMVGCENSKK SDSGSNEDKS LSDDIINLDQ GDPTAFQEYW MKKKDRCTVV IPAWDLMSYF
SDTKNVCWFL EPELEKAIKA LHGAIGNAAT EERYIVVGTG SSQLCQAALF ALSSLSEVKP
VSIVAAVPYY STYVEEASYL QSTLYKWEGD ARTFDKKGPY IELVTSPNNP DGIMREPVVN
RREGGKVIHD LAYYWPHYTP ITRRQDHDLM LFTFSKITGH AGSRIGWALV KDIEVAKKMV
HYLTINSIGV SKESQTRATT ILNELTKTCR TQSESFFEYG YEKMKSRWER LREVVESGDA
FTLPNYPQDF CNFFGKTLST SPAFAWLGYK EERDLGSLLK EKKVLTRGGD RCGCNKRYVR
VSMLSRDDDF DVSLQRLATI KDLKCVEP
