ID   TNAA_KLEAE              Reviewed;         462 AA.
AC   Q59342;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
GN   Name=tnaA;
OS   Klebsiella aerogenes (Enterobacter aerogenes).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=548;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SM-18;
RX   PubMed=7510326; DOI=10.1099/00221287-140-4-999;
RA   Kawasaki K., Yokota A., Oita S., Kobayashi C., Yoshikawa S., Kawamoto S.,
RA   Takao S., Tomita F.;
RT   "Cloning and characterization of a tryptophanase gene from Enterobacter
RT   aerogenes SM-18.";
RL   J. Gen. Microbiol. 139:3275-3281(1993).
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.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000305}.
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DR   EMBL; D14297; BAA03249.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59342; -.
DR   SMR; Q59342; -.
DR   BioCyc; MetaCyc:MON-7541; -.
DR   UniPathway; UPA00332; UER00452.
DR   GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00544; Tryptophanase; 1.
DR   InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR   InterPro; IPR011166; Beta-eliminating_lyase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR013440; TNase.
DR   InterPro; IPR018176; Tryptophanase_CS.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF001386; Trpase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02617; tnaA_trp_ase; 1.
DR   PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Tryptophan catabolism.
FT   CHAIN           1..462
FT                   /note="Tryptophanase"
FT                   /id="PRO_0000195614"
FT   MOD_RES         261
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  51830 MW;  79424F38BAB3A71A CRC64;
     MKRIPEPFRI KMVENIRMTT FDDRVKALKE AGYNPFLLNS QDVYIDLLTD SGTGAMSDHQ
     WAGLMMGDEA YAGSRNYQHL CEKVKEIIGY PYTIPTHQGR GAEQILFPSL IARRKSAHPV
     FISNFHFDTT AAHVELNGAK AINVVTPKAF DTTSWYDWKG NFDIDLLKAT IAEHGAENVA
     AIITTVTCNS SGGQPVSLAN MREVYQIARQ NNIPVVIDSA RFCENAWFIK QREEGYADKS
     VKEIILEMYQ YGDMLTMSAK KDPMVNIGGL CCFRDDEELF NEVRIRCVPM EGFVTYGGLA
     GRDMEALAIG LEEGTNEDYL AYRINQVEYL GERLREGGIP IQYPTGGHAV FVDAKLLLPH
     IPPEQFPAHA LNNELYLEAG IRSVEIGSLL LGRDPETGKQ KASPMELLRL TIPRRVYTND
     HMDYIADALI AVKARAATIK GLTFTYEPPV LRHFVARLKP VK