ID   TNAA_PASMU              Reviewed;         471 AA.
AC   Q9CL27;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
GN   Name=tnaA; OrderedLocusNames=PM1420;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03504.1; -; Genomic_DNA.
DR   RefSeq; WP_005754976.1; NC_002663.1.
DR   AlphaFoldDB; Q9CL27; -.
DR   SMR; Q9CL27; -.
DR   STRING; 747.DR93_274; -.
DR   PRIDE; Q9CL27; -.
DR   EnsemblBacteria; AAK03504; AAK03504; PM1420.
DR   KEGG; pmu:PM1420; -.
DR   HOGENOM; CLU_047223_0_0_6; -.
DR   OMA; EMYQYGD; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000000809; Chromosome.
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; Reference proteome; Tryptophan catabolism.
FT   CHAIN           1..471
FT                   /note="Tryptophanase"
FT                   /id="PRO_0000195616"
FT   MOD_RES         270
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   471 AA;  52893 MW;  B6DE142FF1A7BF8E CRC64;
     MENFKHLPEP FRIRVIEPVR RTTRSYREEA ILKAGMNPFL LDSEDVFIDL LTDSGTGAVT
     QEMQAAMLRG DEAYSGSRSY HALANAVKEI FGYEYTIPTH QGRGAEQIYI PVLIKKREQE
     KGLDRSKMVV FSNYFFDTTQ GHSQINGATV RNVYTKEAFD TSVNADFKGD FDLEKLEQGI
     QEVGAENVPY IVCTITCNSA GGQPVSLANM RAMYEIAKKY DIPVVMDSAR FAENAYFIQQ
     REPGYKEWTI EQITYESYKY ADALAMSAKK DAMVPMGGLL CFKDKSMEDV YNECRTLCVV
     QEGFPTYGGL EGGAMERLAV GLRDGMRQDW LAYRINQIEY LVNGLEAIGV VCQQPGGHAA
     FVDAGKLLPH IPADQFPAQA LACELYKVAG IRAVEIGSFL LGRDPKTGKQ LPCPAELLRL
     TIPRATYTQT HMDFIIEAFK QVKENAENIK GLTFTYEPKV LRHFTARLKE V