ID   TRPB_CORGB              Reviewed;         417 AA.
AC   A4QI76;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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}; OrderedLocusNames=cgR_2920;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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; AP009044; BAF55942.1; -; Genomic_DNA.
DR   RefSeq; WP_011898116.1; NC_009342.1.
DR   AlphaFoldDB; A4QI76; -.
DR   SMR; A4QI76; -.
DR   EnsemblBacteria; BAF55942; BAF55942; cgR_2920.
DR   KEGG; cgt:cgR_2920; -.
DR   HOGENOM; CLU_016734_3_1_11; -.
DR   OMA; GPEHAMF; -.
DR   PhylomeDB; A4QI76; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000006698; 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..417
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000018334"
FT   MOD_RES         99
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   417 AA;  44813 MW;  62AA1E857A63C680 CRC64;
     MTEKENLGGS TLLPAYFGEF GGQFVAESLL PALDQLEKAF VDATNSPEFR EELGGYLRDY
     LGRPTPLTEC SNLPLSGEGK GFARIFLKRE DLVHGGAHKT NQVIGQVLLA KRMGKTRIIA
     ETGAGQHGTA TALACALMGL ECVVYMGAKD VARQQPNVYR MQLHGAKVIP VESGSGTLKD
     AVNEALRDWT ATFHESHYLL GTAAGPHPFP TIVREFHKVI SEEAKAQMLE RTGKLPDVVV
     ACVGGGSNAI GMFADFIDDE GVELVGAEPA GEGLDSGKHG ATITNGQIGI LHGTRSYLMR
     NSDGQVEESY SISAGLDYPG VGPQHAHLHA TGRATYVGIT DAEALQAFQY LARYEGIIPA
     LESSHAFAYA LKRAKTAEEE GQNLTILVSL SGRGDKDVDH VRRTLEENPE LILKDNR