ID   TRPB_PSESY              Reviewed;         408 AA.
AC   P34817;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Pseudomonas syringae pv. syringae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8423001; DOI=10.1016/0378-1119(93)90534-a;
RA   Auerbach S., Gao J., Gussin G.N.;
RT   "Nucleotide sequences of the trpI, trpB, and trpA genes of Pseudomonas
RT   syringae: positive control unique to fluorescent pseudomonads.";
RL   Gene 123:25-32(1993).
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; M95710; AAA26014.1; -; Genomic_DNA.
DR   PIR; JQ2126; JQ2126.
DR   AlphaFoldDB; P34817; -.
DR   SMR; P34817; -.
DR   PRIDE; P34817; -.
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..408
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098986"
FT   MOD_RES         97
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   408 AA;  44508 MW;  3538C72897D9CAB8 CRC64;
     MTQSQTDLRN GPDATGMFGA FGGRYVAETL MPLILDLARE YEAAKEDPAF KEELAYFQRD
     YVGRPSPLYF AERLTEFCGG AKIYLKREEL NHTGAHKINN CIGQILLARR MGKKRIIAET
     GAGMHGVATA TVAARFGLQC VIYMGTTDIE RQQANVFRMK LLGAEVIPVV AGTGTLKDAM
     NEALRDWVTN VEDTFYLIGT VAGPHPYPAM VRDFQAVIGK ETRDQLQAQE GRLPDSLVAC
     IGGGSNAMGL FHPFLDDKSV EIIGVEAAGH GIETGKHAAS LNGGVPGVLH GNRTFLLQDD
     DGQIIDAHSI SAGLDYPGIG PEHAWLHDIG RVQYTSVTDD EALDAFHKCC RLEGIIPALE
     SAHALAEVFK RAPTLPKDHL MVVNLSGRGD KDMQTVMHHM ETTKQEKH