ID   TRPB_CAMJJ              Reviewed;         392 AA.
AC   A1VY69;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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};
GN   OrderedLocusNames=CJJ81176_0372;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) 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}.
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DR   EMBL; CP000538; EAQ73016.1; -; Genomic_DNA.
DR   RefSeq; WP_002854204.1; NC_008787.1.
DR   AlphaFoldDB; A1VY69; -.
DR   SMR; A1VY69; -.
DR   STRING; 354242.CJJ81176_0372; -.
DR   EnsemblBacteria; EAQ73016; EAQ73016; CJJ81176_0372.
DR   KEGG; cjj:CJJ81176_0372; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_7; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000646; Chromosome.
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..392
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000018332"
FT   MOD_RES         84
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   392 AA;  42947 MW;  3423FB3035C50732 CRC64;
     MKKAYYGDFG GQFLPESAMF ALNELEGAFL KFSKDKLFKK ELNELLKTYV GRPTPLYFAR
     NLSKKYQHEI YLKREDLNHT GAHKINNAIA QALLAKKMGK KKIIAETGAG QHGLATATAA
     ALLGLECEIY MGATDVQRQA LNVYKMELLG AKIHAVQSGL KTLKEATTAA IQAWVGDIKN
     IFYVVGSAVG PYPYPKMVMH FQSIIGKECK MQLQKLNKKV DYIIAAVGGG SNAAGIFYDF
     IKDENVKLIG IEAGGLGIDT PYHAATLNKG KTGIIHGMKT KVLQDDLGNI LPVHSVSAGL
     DYPGIGPLHA FLFESKRAQY HAISDEECMQ ALKLLCKEEG IIAAIESSHA LAFLEKLCPT
     LKKKSVIVVN LSGRGDKDMQ MIRDYKKGVI YG