ID   TRPB_PSEPU              Reviewed;         405 AA.
AC   P11080;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPG1 C1S;
RX   PubMed=2503057; DOI=10.1016/0300-9084(89)90183-1;
RA   Eberly L., Crawford I.P.;
RT   "DNA sequence of the tryptophan synthase genes of Pseudomonas putida.";
RL   Biochimie 71:521-531(1989).
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; X13299; CAA31661.1; -; Genomic_DNA.
DR   PIR; S03835; B30768.
DR   RefSeq; WP_015268451.1; NZ_RJAI01000071.1.
DR   AlphaFoldDB; P11080; -.
DR   SMR; P11080; -.
DR   STRING; 1240350.AMZE01000007_gene2747; -.
DR   GeneID; 58533700; -.
DR   GeneID; 66675447; -.
DR   eggNOG; COG0133; Bacteria.
DR   OrthoDB; 912282at2; -.
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..405
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098982"
FT   MOD_RES         95
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  44047 MW;  B213EB22022A8EF0 CRC64;
     MTQSQYRPGP DANGLFGSFG GRYVAETLMP LVLDLAREYE AAKADPKFLE ELAYFQRDYI
     GRPNPLYFAE RLTEHCGGAK IFFKREELNH TGAHKVNNCI GQVLLAKRMG KKRLIAETGA
     GMHGVATATV AARFGLPCVI YMGATDIERQ QANVFRMKLL GAEIVPVTAG TGTLKDAMNE
     ALRDWVTNVE DTFYLIGTVA GPHPYPAMVR DFQSIIGKET RAQLQEKEGR LPDSLVACVG
     GGSNAMGLFH EFLEEPSVQI IGVEAGGHGV HTDKHAASLN GGVPGVLHGN RTYLLQDEDG
     QITDAHSISA GLDYPGIGPE HAYLHEVKRV EYVSITDDEA LDAFHATCRL EGIIPALESS
     HALAEAIKRA PKLPKDHLMV VCLSGRGDKD MQTVMNHMAA QEKQA