ID   TRPB_CAMAC              Reviewed;         466 AA.
AC   O50046;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Tryptophan synthase beta chain 2, chloroplastic;
DE            EC=4.2.1.20;
DE   Flags: Precursor;
GN   Name=TSB;
OS   Camptotheca acuminata (Happy tree).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Cornales; Nyssaceae; Camptotheca.
OX   NCBI_TaxID=16922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Lu H., McKnight T.D.;
RL   Submitted (JAN-1998) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF042321; AAB97526.1; -; Genomic_DNA.
DR   EMBL; AF042320; AAB97087.1; -; mRNA.
DR   AlphaFoldDB; O50046; -.
DR   SMR; O50046; -.
DR   PRIDE; O50046; -.
DR   UniPathway; UPA00035; UER00044.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
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; Transit peptide;
KW   Tryptophan biosynthesis.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..466
FT                   /note="Tryptophan synthase beta chain 2, chloroplastic"
FT                   /id="PRO_0000035785"
FT   MOD_RES         161
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  51265 MW;  63E58C46AB6515FE CRC64;
     MAVYTNPACR TNTSAFPGPY RPYSNPSRFS FNLDKFRPRT SAIKVPSICC TIAREMEKER
     SEREPDVLQR PDSFGRFGKF GGKYVPETLM YALTELESAF RSLSGDQVFQ KELDGILKDY
     VGRESPLYFA ERLTLHYKRP NGEGPEIYLK REDLNHTGAH KINNAVAQAL LAKRLGKKRI
     IAETGAGQHG VATATVCARF GLQCVIYMGA QDMERQALNV FRMRLLGAEV RAVHSGTATL
     KDATSEAIRD WVTNVESTHY ILGSVAGPHP YPMMVREFHA VIGKETRKQA LEKWGGKPDV
     LVACVGGGSN AMGLFHEFVD DKDVRMIGVE AAGFGLDSGK HAATLTKGEV GVLHGAMSYL
     LQDDDGQIIE PHSISAGLDY PGVGPEHSFL KDIGRAEYYC CTDEEALEAF KRLSRLEGII
     PALETSHALA FLEKLCPTLP NGTKVVLNCS GRGDKDVHTA IKHLQV