ID   TRPB1_VIBPA             Reviewed;         396 AA.
AC   P22097;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 2.
DT   25-MAY-2022, entry version 147.
DE   RecName: Full=Tryptophan synthase beta chain 1;
DE            EC=4.2.1.20;
GN   Name=trpB1; Synonyms=trpB; OrderedLocusNames=VP1960;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB22;
RX   PubMed=1773058; DOI=10.3109/10425179109020770;
RA   Crawford I.P., Han C.Y., Silverman M.;
RT   "Sequence and features of the tryptophan operon of Vibrio
RT   parahemolyticus.";
RL   DNA Seq. 1:189-196(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; X17149; CAA35035.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC60223.1; -; Genomic_DNA.
DR   RefSeq; NP_798339.1; NC_004603.1.
DR   RefSeq; WP_005481609.1; NC_004603.1.
DR   AlphaFoldDB; P22097; -.
DR   SMR; P22097; -.
DR   STRING; 223926.28806952; -.
DR   EnsemblBacteria; BAC60223; BAC60223; BAC60223.
DR   GeneID; 1189471; -.
DR   KEGG; vpa:VP1960; -.
DR   PATRIC; fig|223926.6.peg.1875; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_6; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002493; Chromosome 1.
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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..396
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000099019"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        25
FT                   /note="K -> E (in Ref. 1; CAA35035)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  43026 MW;  D189578FF0FAF0D4 CRC64;
     MAKLNAYFGE YGGQYVPQIL VPALKQLEQA FIDAQEDPEF RSEFMTLLQE YAGRPTALTL
     TRNLTKGTKT KLYLKREDLL HGGAHKTNQV LGQALLAKRM GKHEIIAETG AGQHGVATAL
     ACALLGLKCR VYMGAKDVER QSPNVFRMKL MGAEVIPVHS GSATLKDACN EALRDWSGSY
     EDAHYLLGTA AGPHPFPTIV REFQRMIGEE TKNQILAREG RLPDAVIACV GGGSNAIGMF
     ADFIEEESVR LIGVEPAGKG IDTDQHGAPL KHGKTGIFFG MKAPLMQDEN GQVEESYSVS
     AGLDFPSVGP QHAHLNAIGR AEYDNVTDDE ALEAFQELAR SEGIIPALES SHALAHALRM
     ARENPEKEQL LVVNLSGRGD KDIFTVHAIL EEKGVI