ID   TNAA_RHOCA              Reviewed;         454 AA.
AC   O30971;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
GN   Name=tnaA;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 938 / 37b4;
RX   PubMed=9765573; DOI=10.1128/jb.180.20.5413-5420.1998;
RA   Cortez N., Carrillo N., Pasternak C., Balzer A., Klug G.;
RT   "Molecular cloning and expression analysis of the Rhodobacter capsulatus
RT   sodB gene, encoding an iron superoxide dismutase.";
RL   J. Bacteriol. 180:5413-5420(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   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000305}.
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DR   EMBL; AF022932; AAC64208.1; -; Genomic_DNA.
DR   PIR; T45297; T45297.
DR   RefSeq; WP_055210628.1; NZ_QKZO01000003.1.
DR   AlphaFoldDB; O30971; -.
DR   SMR; O30971; -.
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   PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Tryptophan catabolism.
FT   CHAIN           1..454
FT                   /note="Tryptophanase"
FT                   /id="PRO_0000195620"
FT   MOD_RES         256
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   454 AA;  50070 MW;  4E7983536A713DBE CRC64;
     MKTIIEPFRI KSVEPIRLTS RPERERLARA AGYNLFGLHS DDVLIDLLTD SGTGAMSSLQ
     WAAVMQGDES YAGSPSFFRF EAAVQNLMPF KHIIPTHQGR AAEAILFSIF GGKGRRIPSN
     THFDTTRGNI EASGATGDDL VIAEGKDPQN LHPFKGNMDL ARLEAYLEAH HAEVPLVMIT
     ITNNAGGGQP VSLANIRAVA DLAHRYGKPF VIDGCRFAEN AWFIKTREEG QADRSIPEIV
     RDCFAVADGM TMSAKKDAFG NIGGWLALND DDLAEEARGH LIRTEGFPTY GGLAGRDLDA
     LAQGLVEIVD EDYLRYRIRT HQYIVERLDA MGVPVVKPAG GHAVFIDARA WLSHIPPLEY
     PGQALAVALY EIAGVRSCEI GTAMFGRQPD GSEKPAAMDL VRLAFPRRTY TQSHADYIVE
     AFEELAATKD ALRGYRIVKE PKLMRHFTCR FEKL