ID   TRPB_BUCDN              Reviewed;         397 AA.
AC   O68428;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Buchnera aphidicola subsp. Diuraphis noxia.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9625791; DOI=10.1007/s002849900337;
RA   Baumann L., Baumann P., Moran N.A.;
RT   "The endosymbiont (Buchnera) of the aphid Diuraphis noxia contains all the
RT   genes of the tryptophan biosynthetic pathway.";
RL   Curr. Microbiol. 37:58-59(1998).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000250}.
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         Evidence={ECO:0000250};
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
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DR   EMBL; AF038565; AAC27735.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68428; -.
DR   SMR; O68428; -.
DR   STRING; 118101.ATN01_01380; -.
DR   UniPathway; UPA00035; UER00044.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Tryptophan biosynthesis.
FT   CHAIN           1..397
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098929"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  43851 MW;  432A0904B7AFFF39 CRC64;
     MTLLNPYFGK FGGMYVPQIL MPALLELEKN FVEAQKDINF HKTFFNLLKN YAGRPTPLTL
     CNNLTKGTKT RIYLKREDLL HGGAHKTNQV LGQAILAIRM KKNEIIAETG AGQHGVATAI
     ACALLNLKCR IYMGIKDIKR QHPNVFRMKL MGAEVIPVKN GSGTLKDACN EALRDWSNSY
     KNSHYMIGTA AGPHPYPTIV REFQKIIGEE TKQQILEQET KLPNAIIACV GGGSNAIGIF
     SNFINDKEVS LIGVEPGGKG IKTGQHGAPL KHGRTGIFFG MKSHLMQDQE GQIQESWSIS
     AGLDFPSVGP EHAWLNSINR AQYVSITDQE ALDTFQLLCK KEGIIPALES SHALAYALKL
     MNLSPKKEQI FVVNLSGRGD KDIFTVHDIL KKTGKRI