ID   TRPB_CORGL              Reviewed;         417 AA.
AC   P06561;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=Cgl3034, cg3363;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3808947; DOI=10.1093/nar/14.24.10113;
RA   Matsui K., Sano K., Ohtsubo E.;
RT   "Complete nucleotide and deduced amino acid sequences of the Brevibacterium
RT   lactofermentum tryptophan operon.";
RL   Nucleic Acids Res. 14:10113-10114(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(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; X04960; CAA28627.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAC00428.1; -; Genomic_DNA.
DR   EMBL; BX927157; CAF18974.1; -; Genomic_DNA.
DR   PIR; F24723; F24723.
DR   RefSeq; NP_602227.1; NC_003450.3.
DR   RefSeq; WP_004567953.1; NC_006958.1.
DR   AlphaFoldDB; P06561; -.
DR   SMR; P06561; -.
DR   STRING; 196627.cg3363; -.
DR   KEGG; cgb:cg3363; -.
DR   KEGG; cgl:Cgl3034; -.
DR   PATRIC; fig|196627.13.peg.2968; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_11; -.
DR   OMA; GPEHAMF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000582; 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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..417
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098946"
FT   MOD_RES         99
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        203
FT                   /note="A -> R (in Ref. 1; CAA28627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323..350
FT                   /note="PQHAHLHATGRATYVGITDAEALQAFQY -> HSTHTCTPPARTTLVSPTPK
FT                   PSKHSSS (in Ref. 1; CAA28627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360..370
FT                   /note="ALESSHAFAYA -> RTGILTRVRLR (in Ref. 1; CAA28627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401..403
FT                   /note="VRR -> RAG (in Ref. 1; CAA28627)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   417 AA;  44797 MW;  2F49AC7CC6C84DD4 CRC64;
     MTEKENLGGS TLLPAYFGEF GGQFVAESLL PALDQLEKAF VDATNSPEFR EELGGYLRDY
     LGRPTPLTEC SNLPLAGEGK 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