ID   TNAA_CLOTE              Reviewed;         472 AA.
AC   Q894M8;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Tryptophanase {ECO:0000255|HAMAP-Rule:MF_00544};
DE            EC=4.1.99.1 {ECO:0000255|HAMAP-Rule:MF_00544};
DE   AltName: Full=L-tryptophan indole-lyase {ECO:0000255|HAMAP-Rule:MF_00544};
DE            Short=TNase {ECO:0000255|HAMAP-Rule:MF_00544};
GN   Name=tnaA {ECO:0000255|HAMAP-Rule:MF_00544}; OrderedLocusNames=CTC_01509;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00544};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00544};
CC   -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC       pathway; indole and pyruvate from L-tryptophan: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00544}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00544}.
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00544}.
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DR   EMBL; AE015927; AAO36064.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q894M8; -.
DR   SMR; Q894M8; -.
DR   STRING; 212717.CTC_01509; -.
DR   PRIDE; Q894M8; -.
DR   EnsemblBacteria; AAO36064; AAO36064; CTC_01509.
DR   KEGG; ctc:CTC_01509; -.
DR   HOGENOM; CLU_047223_0_0_9; -.
DR   OMA; MFPHIPY; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000001412; 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   PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome; Tryptophan catabolism.
FT   CHAIN           1..472
FT                   /note="Tryptophanase"
FT                   /id="PRO_0000195610"
FT   MOD_RES         271
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ   SEQUENCE   472 AA;  53131 MW;  EA84AC3AEB3752CC CRC64;
     MIIYYLKLEG FNMKIKYVAE PFRIKMVEPI KMLTREEREL KIAEAKYNTF NLRGEDVYID
     LLTDSGTNAM SDDQWAGVMK GDEAYAGGKS YFKLVDAVKD IFGYKFVQPV HQGRAAEKVL
     FGLLLGEGKY SISNMHFDTT RAHVELSGAR AIDCVVPEAS DPTVRIPFKG NMDVEKLEKL
     IKEHGADKIG VVVMTITNNS AGGQPVSIEN MKETAEICKK YNIRLCIDAA RYAENAYFIK
     QREPGYENKS IKEIIKEIFS YADIFTMSAK KDAIVNMGGL LGIKEDEELF QLCKGRTISF
     EGFITYGGLS GRDLESLAIG LYEGIDENYL RYRIGQMEYL AARLDEAGIA YQSPVGGHGV
     FVDAKSMFPH IPYNEFPGQV LAVELYKEAG IRTCEIGSYM LGNDPDTGEQ LKADFEFTRL
     AIARRVYTQA HIDIMADALI TIKERANTVK GYRITWEPPI LRHFQASLEP LK