ID   TNAA_HAEIF              Reviewed;         472 AA.
AC   O07674;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
GN   Name=tnaA;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Eagan / Serotype B;
RX   PubMed=9422600; DOI=10.1128/jb.180.1.107-118.1998;
RA   Martin K., Morlin G., Smith A., Nordyke A., Eisenstark A., Golomb M.;
RT   "The tryptophanase gene cluster of Haemophilus influenzae type b: evidence
RT   for horizontal gene transfer.";
RL   J. Bacteriol. 180:107-118(1998).
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   -!- MISCELLANEOUS: Some pathogenic strains of H.influenzae are active in
CC       tryptophan catabolism and contains tna genes which appear to have been
CC       inserted as a mobile unit.
CC   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000305}.
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DR   EMBL; AF003252; AAB96579.1; -; Genomic_DNA.
DR   RefSeq; WP_005658448.1; NZ_VOFW01000014.1.
DR   AlphaFoldDB; O07674; -.
DR   SMR; O07674; -.
DR   PRIDE; O07674; -.
DR   GeneID; 66615542; -.
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..472
FT                   /note="Tryptophanase"
FT                   /id="PRO_0000195615"
FT   MOD_RES         270
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   472 AA;  53089 MW;  8DE063F4D89F04E2 CRC64;
     MENFKHLPEP FRIRVIEPVK RTTREYREQA ILKSGMNPFL LDSEDIFIDL LTDSGTGAVT
     QDMQAAMLRG DEAYSGSRSY YALAKAVKDI FGYEYTIPTH QGRGAEQIYI PVLIAKRERE
     KGLDRSKMVV FSNYFFDTTQ GHSQINGATV RNVYIKEAFD TTAKHPFKGN FDLEKLEKGI
     QEAGAHNVPY IVCTITCNSA GGQPVSIANL KGMYEIARKY DIPVIMDSAR FAENAYFVQQ
     REEAYKDWTI EQITYESYRY ADGLAMSAKK DAMVPMGGIL AFKDKSMEEV YHECRTLCVV
     QEGFPTYGGL EGGAMERLAV GLHDGMRQEW LAYRIAQIEY LVAGLEKIGV LCQQPGGHAA
     FVDAGKLLPH IPADQFPAQA LSCELYKVAG IRAVEIGSFL LGRDPKTGKQ LPCPAELLRL
     TVPRATYTQT HMDFIIEAFQ KVKENAENIK GLTFTYEPKV LRHFTARLKE VE