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   27-MAR-2024, entry version 121.
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};
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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.Q9LR29; -.
DR   PaxDb; 3702-AT1G23320-1; -.
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; AT1G23320; TAR1.
DR   eggNOG; ENOG502QTGD; Eukaryota.
DR   HOGENOM; CLU_036760_1_0_1; -.
DR   InParanoid; Q9LR29; -.
DR   OMA; TIVICFR; -.
DR   OrthoDB; 1275724at2759; -.
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   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:0009851; P:auxin biosynthetic process; IEA:UniProtKB-UniPathway.
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   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 2.10.25.30; EGF-like, alliinase; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR43795:SF22; TRYPTOPHAN AMINOTRANSFERASE-RELATED PROTEIN 1; 1.
DR   Pfam; PF04864; Alliinase_C; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q9LR29; AT.
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
//