AC   MF_00133;
DC   Protein; auto
TR   HAMAP; MF_00133; -; 1; level=0
XX
Names: Trp_synth_beta
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ID   TRPB
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
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CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine.
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the TrpB family.
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DR   Pfam; PF00291; PALP; 1; trigger=no
DR   NCBIfam; TIGR00263; TrpB; 1; trigger=no
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1; trigger=no
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KW   Amino-acid biosynthesis
KW   Aromatic amino acid biosynthesis
KW   Tryptophan biosynthesis
KW   Pyridoxal phosphate
KW   Lyase
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GO   GO:0004834; F:tryptophan synthase activity
GO   GO:0000162; P:tryptophan biosynthetic process
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FT   From: TRPB_ECOLI (P0A879)
FT   MOD_RES         87
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
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Size: 388-459;
Related: None;
Template: P0A2K1; P0A879; Q8U093;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in AERPE, NOSS1, AQUAE, ARCFU, COREF, VIBPA, WOLSU, METTH, PYRAB,
 PYRFU, THEMA
Plasmid: None
Comments: Highly divergent CHLTR; sequence not included in alignment.
 Duplicated trpB seems of archaebacterial origin. Some archaea have only
 such form (AERPE), some have only the classical form (METJA) and some
 have both including two bacteria (AQUAE and THEMA).
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# Revision 1.44 2023/06/01
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