TRPB1_ARATH
ID TRPB1_ARATH Reviewed; 470 AA.
AC P14671;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Tryptophan synthase beta chain 1, chloroplastic;
DE EC=4.2.1.20;
DE Flags: Precursor;
GN Name=TSB1; OrderedLocusNames=At5g54810; ORFNames=MBG8.7;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2734310; DOI=10.1073/pnas.86.12.4604;
RA Berlyn M.B., Last R.L., Fink G.R.;
RT "A gene encoding the tryptophan synthase beta subunit of Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4604-4608(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
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DR EMBL; M23872; AAA32878.1; -; Genomic_DNA.
DR EMBL; AB005232; BAB08760.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96543.1; -; Genomic_DNA.
DR EMBL; AF367264; AAK56253.1; -; mRNA.
DR EMBL; AY133620; AAM91450.1; -; mRNA.
DR EMBL; AY087382; AAM64932.1; -; mRNA.
DR PIR; A33929; A31393.
DR RefSeq; NP_200292.1; NM_124862.5.
DR AlphaFoldDB; P14671; -.
DR SMR; P14671; -.
DR BioGRID; 20815; 5.
DR IntAct; P14671; 1.
DR STRING; 3702.AT5G54810.1; -.
DR PaxDb; P14671; -.
DR PRIDE; P14671; -.
DR ProteomicsDB; 232385; -.
DR EnsemblPlants; AT5G54810.1; AT5G54810.1; AT5G54810.
DR GeneID; 835571; -.
DR Gramene; AT5G54810.1; AT5G54810.1; AT5G54810.
DR KEGG; ath:AT5G54810; -.
DR Araport; AT5G54810; -.
DR TAIR; locus:2160190; AT5G54810.
DR eggNOG; KOG1395; Eukaryota.
DR HOGENOM; CLU_016734_3_1_1; -.
DR InParanoid; P14671; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 591064at2759; -.
DR PhylomeDB; P14671; -.
DR BioCyc; ARA:AT5G54810-MON; -.
DR BioCyc; MetaCyc:AT5G54810-MON; -.
DR BRENDA; 4.2.1.20; 399.
DR UniPathway; UPA00035; UER00044.
DR PRO; PR:P14671; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P14671; baseline and differential.
DR Genevisible; P14671; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0004834; F:tryptophan synthase activity; IDA:TAIR.
DR GO; GO:0009684; P:indoleacetic acid biosynthetic process; TAS:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00263; trpB; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Lyase; Plastid; Pyridoxal phosphate; Reference proteome; Transit peptide;
KW Tryptophan biosynthesis.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..470
FT /note="Tryptophan synthase beta chain 1, chloroplastic"
FT /id="PRO_0000035783"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 470 AA; 50926 MW; 2EA63F685927FEE1 CRC64;
MAASGTSATF RASVSSAPSS SSQLTHLKSP FKAVKYTPLP SSRSKSSSFS VSCTIAKDPP
VLMAAGSDPA LWQRPDSFGR FGKFGGKYVP ETLMHALSEL ESAFYALATD DDFQRELAGI
LKDYVGRESP LYFAERLTEH YRRENGEGPL IYLKREDLNH TGAHKINNAV AQALLAKRLG
KKRIIAETGA GQHGVATATV CARFGLECII YMGAQDMERQ ALNVFRMRLL GAEVRGVHSG
TATLKDATSE AIRDWVTNVE TTHYILGSVA GPHPYPMMVR DFHAVIGKET RKQALEKWGG
KPDVLVACVG GGSNAMGLFH EFVNDTEVRM IGVEAAGFGL DSGKHAATLT KGDVGVLHGA
MSYLLQDDDG QIIEPHSISA GLDYPGVGPE HSFFKDMGRA EYYSITDEEA LEAFKRVSRL
EGIIPALETS HALAYLEKLC PTLSDGTRVV LNFSGRGDKD VQTVAKYLDV
