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TNAA_VIBCH
ID   TNAA_VIBCH              Reviewed;         472 AA.
AC   Q9KN05; O86039;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Tryptophanase;
DE            EC=4.1.99.1;
DE   AltName: Full=L-tryptophan indole-lyase;
DE            Short=TNase;
GN   Name=tnaA; OrderedLocusNames=VC_A0161;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-241.
RC   STRAIN=Bengal;
RA   Tang T.H., Ravichandran M., Johari M.R., Zainuddin Z.F.;
RT   "Vibrio cholerae putative tryptophanase gene partial cds.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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; AE003853; AAF96074.1; -; Genomic_DNA.
DR   EMBL; AF081274; AAC33284.1; -; Genomic_DNA.
DR   PIR; B82492; B82492.
DR   RefSeq; NP_232561.1; NC_002506.1.
DR   RefSeq; WP_000427054.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KN05; -.
DR   SMR; Q9KN05; -.
DR   STRING; 243277.VC_A0161; -.
DR   DNASU; 2612777; -.
DR   EnsemblBacteria; AAF96074; AAF96074; VC_A0161.
DR   GeneID; 57741617; -.
DR   KEGG; vch:VC_A0161; -.
DR   PATRIC; fig|243277.26.peg.2799; -.
DR   eggNOG; COG3033; Bacteria.
DR   HOGENOM; CLU_047223_0_0_6; -.
DR   OMA; EMYQYGD; -.
DR   BioCyc; VCHO:VCA0161-MON; -.
DR   UniPathway; UPA00332; UER00452.
DR   Proteomes; UP000000584; Chromosome 2.
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; Reference proteome; Tryptophan catabolism.
FT   CHAIN           1..472
FT                   /note="Tryptophanase"
FT                   /id="PRO_0000195625"
FT   MOD_RES         270
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   472 AA;  52920 MW;  632384F54C06F7B9 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 YTECRTLCVV
     QEGFPTYGGL EGGAMERLAV GLYDGMRQDW LAYRINQVEY LVNGLEAIGV ICQQAGGHAA
     FVDAGKLLPH IPADQFPAHA LACELYKVAG IRAVEIGSLL LGRDPATGKQ HPCPAELLRL
     TIPRATYTQT HMDFIIEAFE KVKANARNVK GLEFTYEPPV LRHFTARLKE KA
 
 
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