ID   TNAA_HALS3              Reviewed;         448 AA.
AC   B0R7Q6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Probable 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=OE_4331R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(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   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00544}.
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DR   EMBL; AM774415; CAP14775.1; -; Genomic_DNA.
DR   RefSeq; WP_012289493.1; NC_010364.1.
DR   AlphaFoldDB; B0R7Q6; -.
DR   SMR; B0R7Q6; -.
DR   PRIDE; B0R7Q6; -.
DR   EnsemblBacteria; CAP14775; CAP14775; OE_4331R.
DR   GeneID; 5953359; -.
DR   KEGG; hsl:OE_4331R; -.
DR   HOGENOM; CLU_047223_0_0_2; -.
DR   OMA; EMYQYGD; -.
DR   PhylomeDB; B0R7Q6; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000001321; 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   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Tryptophan catabolism.
FT   CHAIN           1..448
FT                   /note="Probable tryptophanase"
FT                   /id="PRO_1000128915"
FT   MOD_RES         253
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ   SEQUENCE   448 AA;  48121 MW;  B1AF82C45494C139 CRC64;
     MRSHTATMVD RIEDTSRADR EAALADAGHN VFELASDDVA VDLLTDSGTG TMSNDQWAAM
     LQGDEAYAGS ASFEDLAVAA EDVMGFQHII PAHQGRGAEN VLYGAVLSAG DTVLNNAHFD
     TTRAHVAAND ATPVDCPVDG ARDPDTDAPF KGNFSVERAR RVVDDVGADA VPVVVLTITN
     NSMAGQPVSI ENTREVAAFA DDIDATFVID ACRFAENAHF VQQREPGYEH DSVAAIAREQ
     LSYADACVMS GKKDGLVNVG GFVGLHDDGR LHEQCRQRGI LYEGFSTYGG MSGRDMAAFA
     VGLREAVEPP YVAERVAQVQ RLADALTDRD VPIYQPAGGH AVYIDANAAL PHLPREQFPG
     QAFVCELYRE GGVRAVELGR FAFPDTDRRD LVRLALPRRT YGPDHLDHVA DTAAAVCERG
     TDVTGLEIVS EPELTELRHF SAALQPVA