ID   TRPB_LACCA              Reviewed;         406 AA.
AC   P17167;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2113923; DOI=10.1093/oxfordjournals.jbchem.a123034;
RA   Natori Y., Kano Y., Imamoto F.;
RT   "Nucleotide sequences and genomic constitution of five tryptophan genes of
RT   Lactobacillus casei.";
RL   J. Biochem. 107:248-255(1990).
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; D00496; BAA00386.1; -; Genomic_DNA.
DR   PIR; S42346; JS0343.
DR   AlphaFoldDB; P17167; -.
DR   SMR; P17167; -.
DR   STRING; 543734.LCABL_00730; -.
DR   PRIDE; P17167; -.
DR   eggNOG; COG0133; Bacteria.
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..406
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098958"
FT   MOD_RES         97
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   406 AA;  43675 MW;  CA1A0BEDFFFC3BC8 CRC64;
     MKTLNETTQQ STRAGRYGKD FGGQYIPETL MTELEKVTKA FNDLKDNPEF KAELNDLLVN
     YANRPSLLYY AKNMTEDLGG AKIYLKREDL NHTGAHKINN VIGQALLAKH LGKKRLIAET
     GAGQHGVATA TIAALMGMDC EIFMGKEDTD RQKLNVYRME LLGAKVHPVT SGSMVLKDAV
     NATLQEWASP SDDTFYVLGS AVGPAPFPEM VKHFQSVIST ESKQQLQAKE AQLPDMVVAC
     VGGGSNAIGS FAAYIDDPSV QLVGVEAAGK GADTDRTAAT IERGSVGIFH GMKSLFMQNE
     DGQIDPVYSI SAGLDYPGVG PEHAALAQEG RAQYVGITDD EAVEAFTYIA KQEGIVAAIE
     SCHAIAYVEK IAPQMAKDQI IICTLSGRGD KDVASIAKYK GVDVDE