ID   TRPB_NEIGO              Reviewed;         400 AA.
AC   Q84GJ9;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 71.
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   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=12720087; DOI=10.1007/s00438-002-0799-6;
RA   Jose J., Otto G.W., Meyer T.F.;
RT   "The integration site of the iga gene in commensal Neisseria sp.";
RL   Mol. Genet. Genomics 269:197-204(2003).
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; AY165022; AAN65176.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84GJ9; -.
DR   SMR; Q84GJ9; -.
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..400
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098971"
FT   MOD_RES         92
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   400 AA;  43549 MW;  3765C02F97627ACA CRC64;
     MKNYHAPDEK GFFGEHGGLY VSETLIPALK ELEQAYNEAK NDPEFWAEFR RDLKHYVGRP
     SPVYHAARLS EHLGGAQIWL KREDLNHTGA HKVNNTIGQA LLARRMGKKR VIAETGAGQH
     GVASATVAAR FGMTSDVYMG ADDIQRQMPN VFRMKLLGAN VIGVDSGSRT LKDAMNEAMR
     EWVARVDDTF YIIGTAAGPA PYPEMVRDFQ CVIGNEAKAQ MQEATGRQPD VAVACVGGGS
     NAIGLFYPYI EEENVRLVGV EAGGLDVDTP DHAAPITSGA PIGVLHGFRS YLMQDENGQV
     LGTHSVSAGL DYPGIGPEHS HLHDIKRVEY TVAKDDEALE AFDLLCRFEG IIPALESSHV
     VGSGDKTRRK MGKDQVILVN LSGRGDKDIN TVAKLKGIEL