ID   TNAA_AERPE              Reviewed;         467 AA.
AC   Q9YCI2;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Probable tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
GN   Name=tnaA; OrderedLocusNames=APE_1275;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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   -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000002; BAA80265.1; -; Genomic_DNA.
DR   PIR; C72601; C72601.
DR   AlphaFoldDB; Q9YCI2; -.
DR   SMR; Q9YCI2; -.
DR   STRING; 272557.APE_1275; -.
DR   PRIDE; Q9YCI2; -.
DR   EnsemblBacteria; BAA80265; BAA80265; APE_1275.
DR   KEGG; ape:APE_1275; -.
DR   PATRIC; fig|272557.25.peg.873; -.
DR   eggNOG; arCOG04196; Archaea.
DR   OMA; EMYQYGD; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000002518; 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; Reference proteome; Tryptophan catabolism.
FT   CHAIN           1..467
FT                   /note="Probable tryptophanase"
FT                   /id="PRO_0000195629"
FT   MOD_RES         263
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  52547 MW;  9120862C0F311DB2 CRC64;
     MPILPSPNPP VEPYKIRMVE PIRLLPREER LRRLREAGWN VFRLRSIDIF IDLLTDSGTG
     SMSIYQWAAL MTGDEAYAGA RSWFRFRDAV RDVLGLDLVL PVHQGRAAER ILYGELLRRR
     NARIVPANTH FDTGRAVILN QGGVPLDLPS PQASRREAYP FKGDIDVARL ERLLKERSRD
     VAFILLVITN NTAGGQPVSM DNVKTVRELA DAYGLPLVMD ICRFAENAYL VKERDPRYRG
     WSVRDIAREM ISYGDHFVMS AKKDGLANIG GFIATRDPSL YEDLAARVVL EEGYVTYGGL
     AGRDLEAIAQ GLREVVEEDY LRHRVEQVRY LGELLSSQGV PIVEPVGGHA VYVDVLEALP
     EMPRSHYPAD ALAAALYLES GVRAVGLGAL AFAREENGEI VYPEFELLRL AVPRRTYTNS
     HMEYVAASLA RLLREGRRKV KGLRVVKEPR IKGIRHFLAE LEPIEPV