ID   TRPB_STRP2              Reviewed;         407 AA.
AC   Q04IY9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133}; OrderedLocusNames=SPD_1597;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000255|HAMAP-Rule:MF_00133}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
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DR   EMBL; CP000410; ABJ54918.1; -; Genomic_DNA.
DR   RefSeq; WP_000331283.1; NC_008533.2.
DR   AlphaFoldDB; Q04IY9; -.
DR   SMR; Q04IY9; -.
DR   STRING; 373153.SPD_1597; -.
DR   EnsemblBacteria; ABJ54918; ABJ54918; SPD_1597.
DR   GeneID; 60232623; -.
DR   KEGG; spd:SPD_1597; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_9; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 912282at2; -.
DR   BioCyc; SPNE373153:G1G6V-1727-MON; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001452; 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; Tryptophan biosynthesis.
FT   CHAIN           1..407
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000018409"
FT   MOD_RES         91
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   407 AA;  44258 MW;  01F938ED7929E820 CRC64;
     MAYQEPNKDG FYGKFGGRFV PETLMTAVLE LEKAYRESQA DPSFQEELNQ LLRQYVGRET
     PLYYAKNLTQ HIGGAKIYLK REDLNHTGAH KINNALGQVW LAKRMGKKKI IAETGAGQHG
     VATATAAALF NMECIIYMGE EDVKRQALNV FRMELLGAKV EAVTDGSRVL KDAVNAALRS
     WVANIDDTHY ILGSTLGPHP FPEIVRDFQS VIGREAKQQY RDLTGQNLPD ALVACVGGGS
     NAIGLFHPFV EDESVAMYGA EAAGLGVDTE HHAATLTKGR PGVLHGSLMD VLQDAHGQIL
     EAFSISAGLD YPGIGPEHSH YHDIKRASYV PVTDEEALEG FQLLSRVEGI IPALESSHAI
     AFAVKLAKEL GPEKSMIVCL SGRGDKDVVQ VKDRLEADAA KKGEAHA