ID   TRPB_PSESH              Reviewed;         409 AA.
AC   Q849P2;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 77.
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};
OS   Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS   phaseolicola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1449 / Race 7;
RA   Tsaltas D.;
RT   "Biochemical, structural and molecular characterization of resistant
RT   interactions between Pseudomonas syringae pv. phaseolicola and Phaseolus
RT   vulgaris.";
RL   Thesis (2003), University of London, United Kingdom.
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; AY210847; AAO50076.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q849P2; -.
DR   SMR; Q849P2; -.
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..409
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098984"
FT   MOD_RES         95
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   409 AA;  44542 MW;  D6311A4BB6C9BABF CRC64;
     MTQTNFRSGP DVNGLFGSFG GRYVAETLMP LVLDLNREYE AAKADPEFAK EMAYFQRDYV
     GRPNPLYFAE RLTEFCDGAK IYFKREELNH TGAHKINNCI GQVLLAKRMG KKRLIAETGA
     GMHGVATATV AARFGLPCVI YMGATDIERQ QANVFRMKLL GAEIVPVTSG TGTLKDAMNE
     ALRDWVTNVD DTFYLIGTVA GPHPYPAMVR DFQAIIGKET KEQMQEKEGR LPDSLIACVG
     GGSNAMGLFH PFLDDASVEI IGVEAGGHGV DTDKHAASLN GGVPGVLHGN RTYLLQDGDG
     QITDPHSISA GLDYPGIGPE HAFLHEVKRV EYVSITDDEA LDAFHQCCLL EGIIPALETA
     HALAEAMKRA TNLRDDHLMV VCLSGRGDKD MQTVMNHMAA AEKTQEKLV