AC   MF_00544;
DC   Protein; auto
TR   HAMAP; MF_00544; -; 1; level=0
XX
Names: Tryptophanase
XX
ID   TNAA
case <OC:Bacteria>
DE   RecName: Full=Tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
end case
case <OC:Archaea>
DE   RecName: Full=Probable tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
end case
GN   Name=tnaA;
XX
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-tryptophan = indole + NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:19553, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16881, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; EC=4.1.99.1;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC       pathway; indole and pyruvate from L-tryptophan: step 1/1.
case <OC:Bacteria>
CC   -!- SUBUNIT: Homotetramer.
end case
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
XX
DR   Pfam; PF01212; Beta_elim_lyase; 1; trigger=no
DR   NCBIfam; TIGR02617; tnaA_trp_ase; 1; trigger=no
DR   PROSITE; PS00853; BETA_ELIM_LYASE; 1; trigger=no
XX
case <FT:2> or <FT:3> or <FT:4> or <FT:5>
KW   Acetylation
end case
KW   Lyase
KW   Pyridoxal phosphate
KW   Tryptophan catabolism
XX
GO   GO:0009034; F:tryptophanase activity
GO   GO:0006569; P:tryptophan catabolic process
XX
FT   From: TNAA_ECOLI (P0A853)
FT   MOD_RES         270
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
case <OC:Escherichia> or <OC:Shigella>
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         115
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         156
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         450
FT                   /note="N6-acetyllysine"
FT   Condition: K
end case
XX
Size: 448-473;
Related: MF_00543!;
Template: P0A853; P28796;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in SYMTH
Plasmid: None
Comments: None
XX
# Revision 1.31 2023/06/01
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