TAR4_ARATH
ID TAR4_ARATH Reviewed; 463 AA.
AC Q93Z38; Q9FX14;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Tryptophan aminotransferase-related protein 4;
DE EC=2.6.1.-;
GN Name=TAR4; OrderedLocusNames=At1g34060; ORFNames=F12G12.12, F12G12.150;
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].
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 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 [5]
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; AAG12531.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31667.1; -; Genomic_DNA.
DR EMBL; AY058162; AAL25576.1; -; mRNA.
DR PIR; E86464; E86464.
DR RefSeq; NP_564435.1; NM_103128.4.
DR AlphaFoldDB; Q93Z38; -.
DR SMR; Q93Z38; -.
DR STRING; 3702.AT1G34060.1; -.
DR PaxDb; Q93Z38; -.
DR PRIDE; Q93Z38; -.
DR ProteomicsDB; 234259; -.
DR EnsemblPlants; AT1G34060.1; AT1G34060.1; AT1G34060.
DR GeneID; 840303; -.
DR Gramene; AT1G34060.1; AT1G34060.1; AT1G34060.
DR KEGG; ath:AT1G34060; -.
DR Araport; AT1G34060; -.
DR TAIR; locus:2009031; AT1G34060.
DR eggNOG; ENOG502QQJV; Eukaryota.
DR HOGENOM; CLU_036760_2_0_1; -.
DR InParanoid; Q93Z38; -.
DR OrthoDB; 544719at2759; -.
DR PhylomeDB; Q93Z38; -.
DR PRO; PR:Q93Z38; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93Z38; baseline and differential.
DR Genevisible; Q93Z38; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
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; IPR006947; EGF_alliinase.
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 Pfam; PF04863; EGF_alliinase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Membrane; Pyridoxal phosphate; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..463
FT /note="Tryptophan aminotransferase-related protein 4"
FT /id="PRO_0000411677"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 124
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 239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 259..262
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 282..285
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 293
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT MOD_RES 285
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT CONFLICT 100
FT /note="F -> S (in Ref. 3; AAL25576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 52430 MW; AB0FD34E580AD0BA CRC64;
MMQKKLLLIV SIILNLVFTI HILYYSSTTW NPTWTNRAAA EAETVASFSC SGHGRAFVDG
LGVLDGQKPP CECNNCYIGK DCSVLLKDCP VDANSGDPLF LEPFWMRQAE RSAILVSGWH
RMSYIYEDGT YVSRELEKVI RKLHSVVGNA VTDNRFVIFG SGTTQLLAAA VHALSLTNSS
VSSPARLLTS IPYYAMYKDQ AEFFDSAHLK FEGNASAWKQ SGRNDNITQV IEVVTSPNNP
DGKLKRAVLD GPNVKTLHDY AYYWPHFSPI THPVDEDLSL FSLSKTTGHA GSRFGWGLVK
DKAIYEKMDR FIRLTSMGVS KETQLHVLQL LKVVVGDGGN EIFSFGYGTV KKRWETLNKI
FSMSTRFSLQ TIKPEYCNYF KKVREFTPSY AWVKCERPED TNCYEIFRAA KITGRNGNVF
GSEERFVRLS LIRSQDDFDQ LIAMLKKLVY HEEDVPSENF MYI
