ID   TNAA_SALRD              Reviewed;         471 AA.
AC   Q2S1V4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=SRU_1708;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC45644.1; -; Genomic_DNA.
DR   RefSeq; WP_011404453.1; NC_007677.1.
DR   RefSeq; YP_445827.1; NC_007677.1.
DR   AlphaFoldDB; Q2S1V4; -.
DR   SMR; Q2S1V4; -.
DR   STRING; 309807.SRU_1708; -.
DR   EnsemblBacteria; ABC45644; ABC45644; SRU_1708.
DR   KEGG; sru:SRU_1708; -.
DR   PATRIC; fig|309807.25.peg.1772; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_10; -.
DR   OMA; EMYQYGD; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000008674; 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; Reference proteome; Tryptophan catabolism.
FT   CHAIN           1..471
FT                   /note="Tryptophanase"
FT                   /id="PRO_1000017733"
FT   MOD_RES         256
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ   SEQUENCE   471 AA;  51572 MW;  21D9E446506FBB6C CRC64;
     MDTIIEPFRI KSVEPIQLTS RAERERMIRD AHYNLFNLHA DDVIIDLLTD SGTSAMSAAQ
     WAGLMQGDES YAGSPSYFRF EEAVKDLMPF EHVIPTHQGR AAERILMGIV AGPDAKIPSN
     THFDTTRANI EATGAEAVDL VIDAGHVPDA EHPFKGNINL DRLEALLDAE GDRVPIVMLT
     VTNNTGGGQP VSLANIRGAK ALCDTYDVPL VLDACRFAEN AYFIKQREDG YGDRSVKEIV
     REMFSHADGM TMSAKKDALV NIGGWLALDD DAWARKARNQ LILTEGFPTY GGLAGRDLEA
     IAVGLQEIVD EDYLEYRMAS TRYLGEALTE LGVPIVKPVG GHAVYIDAKS LLPHIPPLDY
     PAQSLAVALY VTGGIRGVEI GSVMFGRQPD GSEEPADQEL LRLAIPRRVY TQSHVDYVIE
     CFEALVGRKG ALCGYEITEE PPQLRHFTAH LRPKAPEAVH HETDGPVEAS S