ID   TRPB_BUCMH              Reviewed;         392 AA.
AC   Q44687;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Buchnera aphidicola subsp. Melaphis rhois.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=118103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10555290; DOI=10.1093/oxfordjournals.molbev.a026071;
RA   Clark M.A., Moran N.A., Baumann P.;
RT   "Sequence evolution in bacterial endosymbionts having extreme base
RT   compositions.";
RL   Mol. Biol. Evol. 16:1586-1598(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-341.
RX   PubMed=8642610; DOI=10.1007/bf02498635;
RA   Rouhbakhsh D., Lai C.-Y., von Dohlen C.D., Clark M.A., Baumann L.,
RA   Baumann P., Moran N.A., Voegtlin D.J.;
RT   "The tryptophan biosynthetic pathway of aphid endosymbionts (Buchnera):
RT   genetics and evolution of plasmid-associated anthranilate synthase (trpEG)
RT   within the aphididae.";
RL   J. Mol. Evol. 42:414-421(1996).
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; AF132318; AAF14254.1; -; Genomic_DNA.
DR   EMBL; L46357; AAB05972.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q44687; -.
DR   SMR; Q44687; -.
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_0000098930"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        316
FT                   /note="Y -> N (in Ref. 2; AAB05972)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  43107 MW;  DD978D787D7CD185 CRC64;
     MTLLNSYFGD FGGMYVPQIL MPALYQLEEE FIFSLKSSKF KIELSNLLEN YAGRPTPLTL
     CRNLTKGTKT KIYLKREDLL HGGAHKTNQV LGQALLAKKM KKKEIIAETG AGQHGVAAAF
     SCALLNLKCR IYMGLKDINR QQQNVFRMKL MGAEVIPVKT GSGTLKDACN EALRDWSENY
     INAHYMLGTA AGPHPYPTIV KEFQSIIGKE TKRQIVREEN CLPNAVIACV GGGSNAIGIF
     SSFISDNSVS LIGVEPGGKG IHTNKHGAPL THGETGIFFG MKTKIMQTEE GQIKESWSIS
     AGLDFPAVGP EHAWLYSTKR AQYVSITDHE AVNAFRCLSK SEGIIPALES SHALAYALKL
     MNNHPQKNQI LIVNISGRGD KDIETVKNFL KM