ID   TRPB_GEOSE              Reviewed;         404 AA.
AC   P19868;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7953 / DSM 5934 / JCM 9488 / NBRC 13737 / NCIB 8157 / NCTC
RC   10007 / NCA 1518;
RA   Ishiwata K., Yoshino S., Iwamori S., Suzuki T., Makiguchi N.;
RT   "Cloning and sequencing of Bacillus stearothermophilus tryptophan synthase
RT   genes.";
RL   Agric. Biol. Chem. 53:2941-2948(1989).
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; D00539; BAA00427.1; -; Genomic_DNA.
DR   PIR; JT0524; JT0524.
DR   AlphaFoldDB; P19868; -.
DR   SMR; P19868; -.
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..404
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098917"
FT   MOD_RES         90
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  44012 MW;  C668F3E3A8DF9FD9 CRC64;
     MERVPNEHGR FGDFGGKFVP ETLMLPLEEI EAELDKALAD ESFKQEYIRI LQHYSGRPTP
     LTFAPNLTRQ LGGAKMYLKR EDLNHTGAHK INNAIGQALL AKRMGKKKLI AETGAGQHGV
     AAATVAAHFG MDCIVFMGEE DIKRQELNVF RMKLLGAEVV PVSSGNRTLK DATNEAIRYW
     VAHCDDHFYM IGSVVGPHPY PKMVREFQRI IGDEAKEQFL ACEGKLPDVI VACVGGGSNA
     IGMFYPFLQD DVRLVGVEAA GKGIDTPYHA ATITKGTKGV IHGAMTYLLQ DEYGQIVEPY
     SISAGLDYPG VGPEHAYLAS IGRVRYESVT DEEAVAAFRL LAQTEGIIPA IESAHAVAKA
     VELAQSMSPD ETVLICLSGR GDKDVQTMMR HLGAKEGEDV AAIR