ID   TRPB_VIBME              Reviewed;         391 AA.
AC   Q9RCE8;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 82.
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   Vibrio metschnikovii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=28172;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RH530;
RA   Kwon Y., Moon S., Kim J., Yoo Y., Rho H.;
RT   "Cloning and sequence analysis of the trpB, trpA and 3'trpC genes of Vibrio
RT   metschinikovii strain RH530.";
RL   Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z19090; CAA79516.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RCE8; -.
DR   SMR; Q9RCE8; -.
DR   PRIDE; Q9RCE8; -.
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..391
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099018"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   391 AA;  42295 MW;  782DFAD978882E70 CRC64;
     MAKLNAYFGE YGGQYVPQIL VPALDQLEQA FIDAQEDPDF RAEFMSLLQE YAGRPTALTL
     TRNLTKGTKT KLYLKREDLL HGGAHKTNEV LGQGLVGKRM GKSAIIAETG AGQHGVGSAL
     ASALVGLKCR IIMGAKNLER QSPNVFRMKL MAESIPSSVT LKVAVNEALR DWSATETTHY
     YLGTAAGPHP YPTIVREFQR IIGEETKLQI LAREGRLPDA VLACIGGGSN AIGMFADFID
     EANVRLIGIE PAGKGIDTHQ HGAPLKHGKT GIFFGMKAPL MQDSYGQVEE SYSVSAGLDF
     PSVGPQHAHL NAIGRANYES ITDDEALEAF QSIARNEGII AALESSHALA YAIKMARIDP
     DKEQLLVVNL SGRGDKDIFT VHQLLEERGA L