ID   TRPB1_COREF             Reviewed;         418 AA.
AC   Q8FLJ6;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Tryptophan synthase beta chain 1;
DE            EC=4.2.1.20;
GN   Name=trpB1; OrderedLocusNames=CE2872;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(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; BA000035; BAC19682.1; -; Genomic_DNA.
DR   RefSeq; WP_006768771.1; NZ_GG700684.1.
DR   AlphaFoldDB; Q8FLJ6; -.
DR   SMR; Q8FLJ6; -.
DR   STRING; 196164.23494716; -.
DR   EnsemblBacteria; BAC19682; BAC19682; BAC19682.
DR   KEGG; cef:CE2872; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_11; -.
DR   OMA; GPEHAMF; -.
DR   OrthoDB; 912282at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001409; 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..418
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000098944"
FT   MOD_RES         99
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   418 AA;  45026 MW;  56E428939AD36D44 CRC64;
     MTDNKNLGGS TLLPAYFGEF GGQFVAESLL PALDQLEKAF VDATNHPEFR QELAAYLRDY
     LGRPTPLTEC SNLPLPGQGR GYARIFLKRE DLVHGGAHKT NQVIGQALLA KRMGKTRIIA
     ETGAGQHGTA TALACSLLGL ECVVYMGAKD VARQQPNVYR MQLHGAKVIP VESGSGTLKD
     AVNEALRDWT ATFHESHYLL GTAAGPHPFP TIVREFHKVI SEEAKAQMLE RTGKMPDVVV
     ACVGGGSNAI GMFADFIDEE GVELVGAEPA GEGLDSGKHG ATITNGQIGI LHGTRSFLMR
     SSDGQVEESY SISAGLDYPG VGPQHAHLHS TGRATYVGIT DAEALIAFQY LARYEGIIAA
     LESSHALAYA LKRAKLAEEE GKQITILVSL SGRGDKDVDH IRRTLEEKPE LILKEEER