ID   TNAA_PROIN              Reviewed;         465 AA.
AC   Q9ZNA8;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
GN   Name=tnaA; Synonyms=tna;
OS   Proteus inconstans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=84631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 12931;
RA   Nishiya Y.;
RT   "DNA encoding the tryptophanase gene and its flanking regions from Proteus
RT   inconstans.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000250};
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; AB019704; BAA34638.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZNA8; -.
DR   SMR; Q9ZNA8; -.
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   PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Tryptophan catabolism.
FT   CHAIN           1..465
FT                   /note="Tryptophanase"
FT                   /id="PRO_0000195618"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  52764 MW;  FCD6A41D96EAF172 CRC64;
     MAKRIVEPFR IKMVENIRIP SREEREVALK EAGYNPFLLP SSAVYIDLLT DSGTTRYDHH
     GSMITGDEAY AGSRNYYDLK DKVKEMFDYD YVIPAHQGRG AENMLFPVLL KVKQEQGGAK
     KPVFISNFHF DTTAAHVELN HCKAINIVTE KAYDSDTYDD WKGNFDIQKL KDNIAPEWCR
     KRCCHYFSIT CNSAGGQPVS MANLKEVYEI AKHHNIFVVM DSARFCENAY FIKERDPKYK
     NATIKEIILD MYKYADALTM SAKKDPLLNI GGLVCIKNDE KIFTLARQRC VPMEGFVTYG
     GLAGRDMAAM VQGLEEGAGE EYLHYRIGQV KYLGDRLREG GISIQYPTGG HAVFVDCKKL
     VPHIPGDQFP AQAVINALYL ESGVRAVEIG SFLLGRDPET GKQKHADMEF MRLTIARRVY
     TNDHMDYIAD ALIGLKDKFA TLKGLDFEYE PPVLRHFTAR LKPIK