TAR1_ORYSJ
ID TAR1_ORYSJ Reviewed; 441 AA.
AC Q0DKE8; A0A0P0WIM5;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Tryptophan aminotransferase-related protein 1 {ECO:0000303|PubMed:22582989};
DE Short=OsTAR1 {ECO:0000303|PubMed:22582989};
DE EC=2.6.1.27 {ECO:0000305};
DE AltName: Full=Protein FISH BONE-LIKE {ECO:0000303|PubMed:24654985};
DE Short=Protein FIB-LIKE {ECO:0000303|PubMed:24654985};
GN Name=TAR1 {ECO:0000303|PubMed:22582989};
GN Synonyms=FBL {ECO:0000303|PubMed:24654985};
GN OrderedLocusNames=Os05g0169300 {ECO:0000312|EMBL:BAF16675.1},
GN LOC_Os05g07720 {ECO:0000305};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=22582989; DOI=10.1111/j.1399-3054.2012.01649.x;
RA Abu-Zaitoon Y.M., Bennett K., Normanly J., Nonhebel H.M.;
RT "A large increase in IAA during development of rice grains correlates with
RT the expression of tryptophan aminotransferase OsTAR1 and a grain-specific
RT YUCCA.";
RL Physiol. Plantarum 146:487-499(2012).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=24654985; DOI=10.1111/tpj.12517;
RA Yoshikawa T., Ito M., Sumikura T., Nakayama A., Nishimura T., Kitano H.,
RA Yamaguchi I., Koshiba T., Hibara K., Nagato Y., Itoh J.;
RT "The rice FISH BONE gene encodes a tryptophan aminotransferase, which
RT affects pleiotropic auxin-related processes.";
RL Plant J. 78:927-936(2014).
CC -!- FUNCTION: Probable tryptophan aminotransferase that may be involved in
CC the regulation of auxin production in developing rice grains.
CC {ECO:0000305|PubMed:22582989}.
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 Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q9S7N2};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in anthers. Expressed at low
CC levels in ovaries. {ECO:0000269|PubMed:24654985}.
CC -!- DEVELOPMENTAL STAGE: During grain filling, expression increases from 4
CC to 20 days after pollination and then decreases to basal levels.
CC {ECO:0000269|PubMed:22582989}.
CC -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAS92467.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC084817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008211; BAF16675.1; -; Genomic_DNA.
DR EMBL; AK071687; BAG92630.1; -; mRNA.
DR EMBL; AP014961; BAS92466.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS92467.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015638820.1; XM_015783334.1.
DR AlphaFoldDB; Q0DKE8; -.
DR SMR; Q0DKE8; -.
DR STRING; 4530.OS05T0169300-01; -.
DR PaxDb; Q0DKE8; -.
DR PRIDE; Q0DKE8; -.
DR EnsemblPlants; Os05t0169300-01; Os05t0169300-01; Os05g0169300.
DR GeneID; 4337930; -.
DR Gramene; Os05t0169300-01; Os05t0169300-01; Os05g0169300.
DR KEGG; osa:4337930; -.
DR eggNOG; ENOG502QPYC; Eukaryota.
DR HOGENOM; CLU_036760_1_0_1; -.
DR InParanoid; Q0DKE8; -.
DR OMA; MMYEAFW; -.
DR OrthoDB; 457006at2759; -.
DR PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR UniPathway; UPA00151; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0050362; F:L-tryptophan:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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 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; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..441
FT /note="Tryptophan aminotransferase-related protein 1"
FT /id="PRO_0000444623"
FT BINDING 110
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 152..153
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 219
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 239..242
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 262..265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 273
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 441 AA; 47349 MW; 40EDFE5DC3F4A6B9 CRC64;
MAAMGSKDGG GGGGGMAAQA GRLGVVASVA FNLAALAFYL RRRYFGGDDA AAVRKKAEAE
VAPSSGKPPV TKDSIINLDH GDPTMYEAFW RGGAGERATI VIPGWQTMSY FSDVGSLCWF
LEPGLEREVR RLHRLVGNAV ADGYHVLVGT GSTQLFQAAL YALSPPGPSA PMNVVSPAPY
YSSYPAVTDF LKSGLYRWAG DAKMFDGDTY VELVCSPSNP DGGIREAVLK SGDGVAVHDL
AYYWPQYTPI TSAAAHDIML FTVSKCTGHA GTRLGWALVK DRAVAQKMSK FIELNTIGVS
KDSQLRAAKI LKAITDGYDR APAAGDDDDD SSRLFHFARR KMVSRWAKLR AAVAASGIFT
LPDELPGHCT FANETVSAYP PFAWLRCGKE GVDDLEGYLR ERKIISRGGG KFGADGRVVR
ISMLDTDEAF AIFVDRLAAM N
