ID   TNAA_AERS4              Reviewed;         461 AA.
AC   A4SNA7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=ASA_2330;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
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; CP000644; ABO90379.1; -; Genomic_DNA.
DR   RefSeq; WP_011898792.1; NC_009348.1.
DR   AlphaFoldDB; A4SNA7; -.
DR   SMR; A4SNA7; -.
DR   STRING; 382245.ASA_2330; -.
DR   EnsemblBacteria; ABO90379; ABO90379; ASA_2330.
DR   KEGG; asa:ASA_2330; -.
DR   PATRIC; fig|382245.13.peg.2284; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_6; -.
DR   OMA; EMYQYGD; -.
DR   OrthoDB; 91973at2; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000000225; 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   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF001386; Trpase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Tryptophan catabolism.
FT   CHAIN           1..461
FT                   /note="Tryptophanase"
FT                   /id="PRO_1000017728"
FT   MOD_RES         261
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ   SEQUENCE   461 AA;  50837 MW;  8C9AF838E44CFC1F CRC64;
     MRRIPEPFRI KMVEPIKQTT GAERRAALEA AGWNPFLLLA EDVYIDLLTD SGTGAMSDRQ
     WAGIMMGDEA YAGSRNFVEL ERTVRELFGY QHVMPTHQGR GAEQILFPEL VKRCKGKAPV
     FISNYHFDTT KAHVELAGER AINLLTPKAL DTTAPYAWKG DFDLGRLTDT IETLGADNVA
     AVIITVTCNS AGGQPVSMGN MQAVSELARR HHIPVVIDAA RFAENAWFIK ARDPDYAKSS
     IKEIVRQMFD LGDMFTMSAK KDGLVNIGGL CCFKEGLDLF RSVQVRCVAM EGFVTYGGLA
     GRDMAALAIG LREGMDEEYL TYRIGQVAYL GERLAEAGIP IQTPTGGHAV FVDAKKLLPH
     IPGEQFPAHA LACALYLEGG VRGVEIGSLL LGRDPATGKQ EAADFELLRL TIPRRVYTRD
     HMDYVADCLI AVKTRASEIR GLTFDYEPPL LRHFTARLKP V