ID   TRPB_BUCSC              Reviewed;         392 AA.
AC   Q59169;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7742976; DOI=10.1111/j.1365-2583.1995.tb00007.x;
RA   Lai C.-Y., Baumann P., Moran N.A.;
RT   "Genetics of the tryptophan biosynthetic pathway of the prokaryotic
RT   endosymbiont (Buchnera) of the aphid Schlechtendalia chinensis.";
RL   Insect Mol. Biol. 4:47-59(1995).
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; U09185; AAA92796.1; -; Genomic_DNA.
DR   RefSeq; WP_075474162.1; NZ_CP011299.1.
DR   AlphaFoldDB; Q59169; -.
DR   SMR; Q59169; -.
DR   STRING; 118110.XW81_01305; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 912282at2; -.
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..392
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098933"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  43033 MW;  5DA5BB394D081F9D CRC64;
     MTLLNSYFGS FGGMYVPQIL MPALYQLESE FVLSLKNLQF KKKLANLLKN YAGRPTPLTL
     CRNLTKGTNT RIYLKREDLL HGGAHKTNQV LGQALLAKQM KKKEIIAETG AGQHGVAAAL
     SCALLNLKCR IYMGIKDIER QKQNVFRMKL MGAQVIPVKS GNGTLKDACN EALRDWSENY
     INAHYMLGTA AGPHPYPTIV KQFQSVIGKE TKQQIFEKEH CLPNSVIACV GGGSNAIGIF
     SSFIEDTSVN LIGVEPGGIG IHTEKHGASL ICGETGIFFG MKSKVMQTHE GQIKESWSIS
     AGLDFPAVGP EHAWLDSIKR VTYVSITDSE AVHAFQHLSK LEGIIPALES SHALAYAIKL
     MNNYPNKNQT LIVNISGRGD KDLKTVEKFL NK