ID   TRPB_MYCIT              Reviewed;         421 AA.
AC   O68905;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Mycobacterium intracellulare.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Batty;
RA   Alavi M.R., Rouse D.A., Morris S.L.;
RT   "Nucleotide sequence and functional analysis of the tryptophan synthase
RT   genes of Mycobacterium intracellulare.";
RL   Submitted (APR-1998) 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: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; AF057042; AAC17134.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68905; -.
DR   SMR; O68905; -.
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..421
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098967"
FT   MOD_RES         110
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   421 AA;  44953 MW;  8D50B7EED86202A1 CRC64;
     MDISPRTRPD LPLPSAAIAE PTRHEPDAGG HFGVYGGRYV AEALMAVIEE VTTAYEKERV
     NQDFLDTLDY LQANYAGRPS PLYEAPRLSE QAGARIFLKR EDLNHTGSHK INNVLGQALL
     AQRMGKKRVI AETGAGQHGV ATATACALLG LECVIYMGAV DTERQALNVA RMRLLGATVV
     SVQSGSKTLK DAINEAFRDW VTNADNTFYC FGTAAGPHPF PAMVRDFQRI IGLEARAQIQ
     AQAGRLPDAV LACIGGGSNA IGIFHPFIDD PGVRLIGFEA AGDGVETGRH AATFSGGSPG
     AFQGSFSYLL QDEDGQTIES HSISAGLDYP GVGPEHAWLR ERVSTTRGWV RNTRGCARFR
     TLCRTEGIIP AIESAHAVAG ALKVAPELGK AAIIVVNLSG RGDKDVETAA QWFGLLGSSD
     R