ID   TRPB_BACAA              Reviewed;         397 AA.
AC   C3P3U0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=BAA_1329;
OS   Bacillus anthracis (strain A0248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=592021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A0248;
RA   Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA   Brettin T.;
RT   "Genome sequence of Bacillus anthracis A0248.";
RL   Submitted (APR-2009) 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; CP001598; ACQ48801.1; -; Genomic_DNA.
DR   RefSeq; WP_001105001.1; NC_012659.1.
DR   AlphaFoldDB; C3P3U0; -.
DR   SMR; C3P3U0; -.
DR   GeneID; 45021253; -.
DR   KEGG; bai:BAA_1329; -.
DR   HOGENOM; CLU_016734_3_1_9; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
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..397
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000198737"
FT   MOD_RES         91
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   397 AA;  43590 MW;  0C56E4584F798313 CRC64;
     MNYAYPDEKG HYGIYGGRYV PETLMQSVLE LEEAYKEAME DEAFQKELNH YLKTYVGRET
     PLYFAENMTE YCGGAKIYLK REDLNHTGAH KINNTIGQAL LAVRMGKKKV VAETGAGQHG
     VATATVCALL GLECVIFMGE EDVRRQKLNV FRMELLGAKV ESVAAGSGTL KDAVNEALRY
     WVSHVHDTHY IMGSVLGPHP FPQIVRDFQS VIGNETKKQY EALEGKLPEA VVACIGGGSN
     AMGMFYPFVH DEEVALYGVE AAGKGVHTEK HAATLTKGSV GVLHGSMMYL LQNEEGQIQE
     AHSISAGLDY PGVGPEHSLL KDIGRVSYHS ITDDEALEAF QLLTKKEGII PALESSHAVA
     YALKLAPQMK EDEGLVICLS GRGDKDVESI KRYMEEV