ID   TNAA_SHESH              Reviewed;         465 AA.
AC   A8G097;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Ssed_3916;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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         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; CP000821; ABV38520.1; -; Genomic_DNA.
DR   RefSeq; WP_012144250.1; NC_009831.1.
DR   AlphaFoldDB; A8G097; -.
DR   SMR; A8G097; -.
DR   STRING; 425104.Ssed_3916; -.
DR   EnsemblBacteria; ABV38520; ABV38520; Ssed_3916.
DR   KEGG; sse:Ssed_3916; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_6; -.
DR   OMA; EMYQYGD; -.
DR   OrthoDB; 91973at2; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000002015; 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..465
FT                   /note="Tryptophanase"
FT                   /id="PRO_1000081943"
FT   MOD_RES         265
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ   SEQUENCE   465 AA;  52163 MW;  02A6779EFF55976C CRC64;
     MKRIPEPFRI KMVESIKMTN LEDREQALTQ AGLNPFLLRS EDVYIDLLTD SGTGAMSDVQ
     WAGLMMGDES YAGSRNYFNL CESVEHFFGY KLTVPVHQGR GAEQILFPCL IERMRQVRGG
     TEPIFISNYH FDTTAGHIEM NGGKALNVVT EKAFDTESYY DWKGDFDLDK LRDTIATYGA
     NNIAAIITTV TCNSSGGQPV SMANMRAVYE IAQKHDIPVV IDSARYCENA YFIKQREPGY
     EDSSMLEIIR EMFQYGDMLT LSAKKDPMVN IGGLCCVRDH EELFRAVQTR CVPMEGFVTY
     GGMAGRDMEA LARGMHEGAD EDFLHYRVCQ VAYLGERLRE AGIPIQYPTG GHAVFVDAAK
     MLPHIPAHQF PAQSLCNALY LEAGIRAVEI GSLLLGREPE TGEQKVSPME LMRLTIPRRV
     YTNDHMDYIA DALIAIKDQA ASLKGLTFDY EPPVLRHFTA KFNSL