ID   TRPB_LACLA              Reviewed;         402 AA.
AC   Q01998;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=LL1463; ORFNames=L0049;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=1400208; DOI=10.1128/jb.174.20.6563-6570.1992;
RA   Bardowski J., Ehrlich S.D., Chopin A.;
RT   "Tryptophan biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL   J. Bacteriol. 174:6563-6570(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; M87483; AAA25228.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK05561.1; -; Genomic_DNA.
DR   PIR; S35129; S35129.
DR   RefSeq; NP_267619.1; NC_002662.1.
DR   RefSeq; WP_010905986.1; NC_002662.1.
DR   AlphaFoldDB; Q01998; -.
DR   SMR; Q01998; -.
DR   STRING; 272623.L0049; -.
DR   PaxDb; Q01998; -.
DR   EnsemblBacteria; AAK05561; AAK05561; L0049.
DR   KEGG; lla:L0049; -.
DR   PATRIC; fig|272623.7.peg.1573; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_9; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002196; Chromosome.
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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..402
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098959"
FT   MOD_RES         91
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  43746 MW;  0F35949CAAE66574 CRC64;
     MTYNQPNNKG FYGQFGGQFV PETLMTAVKQ LEEAYVDSKK DPLFQAELKE LLKDYVGREN
     PLYYAKRLTE YAGGAKIYLK REDLNHTGAH KINNALGQVL LAKKMGKNKV IAETGAGQHG
     VASATAAALF GMECTIYMGE EDVKRQSLNV FRMELLGAKV HSVTDGSRVL KDAVNAALRA
     WVAQVEDTHY VMGSVLGPHP FPQIVRDYQA VIGQEARAQF LEKENKLPDA LVACVGGGSN
     SMGLFYPFVN DESVAMYGVE AAGLGIDTPH HAATITKGRP GVLHGTLMDV LQDENGQMLE
     AFSISAGLDY PGIGPEHSYF NAVGRAKYVD ITDEEALEGF KILSRTEGII PALESSHAIA
     YAVKLAKELG ADKSMIVCLS GRGDKDVVQV KERLEAEKEV KK