ID   TNAA1_SYMTH             Reviewed;         454 AA.
AC   P31014; Q67SB7;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Tryptophanase 1;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase 1;
DE            Short=TNase 1;
GN   Name=tnaA1; Synonyms=tna-1; OrderedLocusNames=STH441;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-36.
RC   STRAIN=IAM 13621;
RX   PubMed=1339259; DOI=10.1128/aem.58.8.2633-2642.1992;
RA   Hirahara T., Suzuki S., Horinouchi S., Beppu T.;
RT   "Cloning, nucleotide sequences, and overexpression in Escherichia coli of
RT   tandem copies of a tryptophanase gene in an obligately symbiotic
RT   thermophile, Symbiobacterium thermophilum.";
RL   Appl. Environ. Microbiol. 58:2633-2642(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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   -!- 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   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD39426.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB010832; BAA24688.1; -; Genomic_DNA.
DR   EMBL; AP006840; BAD39426.1; ALT_INIT; Genomic_DNA.
DR   PIR; A49022; A49022.
DR   AlphaFoldDB; P31014; -.
DR   SMR; P31014; -.
DR   STRING; 292459.STH441; -.
DR   EnsemblBacteria; BAD39426; BAD39426; STH441.
DR   KEGG; sth:STH441; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_9; -.
DR   OMA; EMYQYGD; -.
DR   BioCyc; MetaCyc:MON-7584; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000000417; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Tryptophan catabolism.
FT   CHAIN           1..454
FT                   /note="Tryptophanase 1"
FT                   /id="PRO_0000195622"
FT   MOD_RES         255
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        133
FT                   /note="Missing (in Ref. 1; BAA24688)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  51083 MW;  C13518B3F5CD6555 CRC64;
     MPKGEPFKIK MVEPIRLIPR EDRERALKEA HYNPFFLRSS DVYIDLLTDS GTGAMSQFQW
     SAMMLGDESY AGASSYYRLK ETVTDITGYE YVIPTHQGRG AEKVAFSQLI TRPGMYVLSN
     MFFDTTRGHV QLAGGRPVDL LIDVPTEEYH PFKGNMDTER LEQFIREHGA ENIACIVMTV
     TNNSAGGQPV SMANIRETYQ IARKYGVLVL FDVARYAENC HFIRMREEGY ADKHPIDIAR
     EMFSYGDGLM MSAKKDALVN IGGLLAFRDE ELFTKVGAAV VPFEGFLTYG GLAGRDLEAM
     AVGLREALDP DYLAYRVGQV QYLGEMLRNA GIPIQWPVGG HAVFIDAAKF LPHVPWDQFP
     GHALTLALYL EGGVRTVEVG SLMIGRDPET GENVRGPFEF TRLAIPRRVY TNLHLEDVAE
     TVINAFQKRE EIRGVKFARE PKVLRHFTAW FDPA