ID   TAR3_ARATH              Reviewed;         457 AA.
AC   Q9FE98;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Tryptophan aminotransferase-related protein 3;
DE            EC=2.6.1.-;
GN   Name=TAR3; OrderedLocusNames=At1g34040; ORFNames=F12G12.14, T15K4.10;
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   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).
CC   -!- FUNCTION: Probable aminotransferase. {ECO:0000250|UniProtKB:Q9S7N2}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q9S7N2};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
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DR   EMBL; AC015446; AAG12533.1; -; Genomic_DNA.
DR   EMBL; AC079286; AAG12844.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE31660.1; -; Genomic_DNA.
DR   PIR; C86464; C86464.
DR   RefSeq; NP_174666.1; NM_103126.2.
DR   AlphaFoldDB; Q9FE98; -.
DR   SMR; Q9FE98; -.
DR   STRING; 3702.Q9FE98; -.
DR   PaxDb; 3702-AT1G34040-1; -.
DR   ProteomicsDB; 234153; -.
DR   EnsemblPlants; AT1G34040.1; AT1G34040.1; AT1G34040.
DR   GeneID; 840301; -.
DR   Gramene; AT1G34040.1; AT1G34040.1; AT1G34040.
DR   KEGG; ath:AT1G34040; -.
DR   Araport; AT1G34040; -.
DR   TAIR; AT1G34040; TAR3.
DR   eggNOG; ENOG502QQJV; Eukaryota.
DR   HOGENOM; CLU_036760_2_0_1; -.
DR   InParanoid; Q9FE98; -.
DR   OMA; NDHTFIS; -.
DR   OrthoDB; 1275724at2759; -.
DR   PhylomeDB; Q9FE98; -.
DR   BioCyc; ARA:AT1G34040-MONOMER; -.
DR   PRO; PR:Q9FE98; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FE98; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR006947; EGF_alliinase.
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:SF56; TRYPTOPHAN AMINOTRANSFERASE-RELATED PROTEIN 3; 1.
DR   Pfam; PF04864; Alliinase_C; 1.
DR   Pfam; PF04863; EGF_alliinase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q9FE98; AT.
PE   3: Inferred from homology;
KW   Aminotransferase; Membrane; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..457
FT                   /note="Tryptophan aminotransferase-related protein 3"
FT                   /id="PRO_0000411676"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         123
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         163..164
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         237
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         257..260
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         280..283
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         291
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   MOD_RES         283
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   457 AA;  51654 MW;  61C6E00B734DDE61 CRC64;
     MIHNKLLIAG SIILNLVFTI HILYNNTSTW SPTWTNRAAL EAEAAASVSC SGHGRSYVDG
     LGVLDGHKPC ECHDCYTGKD CSVLLKDCPV DANSGDPLFL EPFWIRKAEE SAVVESGWHR
     MSYTFNGYGL FMSAELEKII RKLHNVVGNA VTDNRFIIFG AGATQLLAAS VHALSQTNSL
     SPSRLVTSVP YYNLYKQQAD FFNSTNLKFE GDASAWKRSE RNDDIKQVIE IVTSPNNPDG
     KLKRAVLDGP NVKYIHDYAY YWPYFSPITR QADEDLSLFS LSKTTGHAGS RFGWALVKEK
     TVYEKMKIYI SLSSMGVSRD TQLRALQLLK VVIGDGGNEI FRFGYGTLKK RWEILNKIFS
     MSTRFSLETI KPEYCNYFKK VREFTPSYAW VKCERPEDTD CYEIFKAAKI TGRNGEMFGS
     DERFVRLSLI RSQDDFDQLI AMLKKFVSKE AVVVDSI
//