ID   TNAA_VIBC3              Reviewed;         472 AA.
AC   A5EYI0; C3M7K1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 78.
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};
GN   OrderedLocusNames=VC0395_1117, VC395_A0154;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(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   -!- 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; CP000626; ABQ18443.1; -; Genomic_DNA.
DR   EMBL; CP001236; ACP10997.1; -; Genomic_DNA.
DR   RefSeq; WP_000427052.1; NZ_JAACZH010000004.1.
DR   AlphaFoldDB; A5EYI0; -.
DR   SMR; A5EYI0; -.
DR   STRING; 345073.VC395_A0154; -.
DR   EnsemblBacteria; ABQ18443; ABQ18443; VC0395_1117.
DR   KEGG; vco:VC0395_1117; -.
DR   KEGG; vcr:VC395_A0154; -.
DR   PATRIC; fig|345073.21.peg.2912; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_6; -.
DR   OMA; EMYQYGD; -.
DR   BRENDA; 4.1.99.1; 15003.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000000249; Chromosome 1.
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   TIGRFAMs; TIGR02617; tnaA_trp_ase; 1.
DR   PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Tryptophan catabolism.
FT   CHAIN           1..472
FT                   /note="Tryptophanase"
FT                   /id="PRO_1000072551"
FT   MOD_RES         270
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ   SEQUENCE   472 AA;  52934 MW;  A382F8849AD161EC CRC64;
     MENFKHLPEP FRIRVIEPVK RTTREYREKA ILNAGMNPFL LDSEDVFIDL LTDSGTGAIT
     QEMQAAMFRG DEAYSGSRSY HALARAVKDI FGYEYTIPTH QGRGAEQIYI PVLIKKREKE
     KGLDRSKMVA LSNYFFDTTQ GHTQINCCVA KNVYTEEAFD TGVKADFKGN FDLEKLEQAI
     LEAGPANVPY IVSTITCNSA GGQPVSIANL KAVYEIAQRY DIPVIMDSAR FAENAYFIQQ
     RERDYRNWSI EEITREAYKY ADGLAMSAKK DAMVQMGGLL CFKDESFFDV YTECRTLCLV
     QEGFPTYGGL EGGAMERLAV GLYDGMRQDW LAYRINQVEY LVNGLEAIGV ICQQAGGHAA
     FVDAGKLLPH IPADQFPAHA LACELYKVAG IRAVEIGSLL LGRDPATGKQ HPCPAELLRL
     TIPRATYTQT HMDFIIEAFE KVKANARNVK GLEFTYEPPV LRHFTARLKE KA