TNAA_VIBVY
ID TNAA_VIBVY Reviewed; 473 AA.
AC Q7MCR1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
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}; OrderedLocusNames=VVA1325;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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; BA000038; BAC97351.1; -; Genomic_DNA.
DR RefSeq; WP_011081771.1; NC_005140.1.
DR AlphaFoldDB; Q7MCR1; -.
DR SMR; Q7MCR1; -.
DR STRING; 672.VV93_v1c42380; -.
DR EnsemblBacteria; BAC97351; BAC97351; BAC97351.
DR GeneID; 66967793; -.
DR KEGG; vvy:VVA1325; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_6; -.
DR OMA; EMYQYGD; -.
DR OrthoDB; 91973at2; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000002675; Chromosome II.
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..473
FT /note="Tryptophanase"
FT /id="PRO_0000195628"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ SEQUENCE 473 AA; 52737 MW; E470BE9719EEEE91 CRC64;
MDNFKHLPEP FRIRVIEPVK RTTREYREEA ILKAGMNPFL LDSEDVFIDL LTDSGTGAIT
QDMQAAMFRG DEAYSGSRSY HALANAVKDI FGYEFTIPTH QGRGAEQIYI PVLIKKREIE
KGLDRSKMVA LSNYFFDTTQ GHTQINCCVA KNVYTEEAFD TGVKADFKGN FDLEKLEEAI
LEAGPANVPY IVSTITCNSA GGQPVSLANL KAVYEIAKRY DIPVIMDSAR FAENAYFIQQ
REKDYQNWSI EEITRESYKY ADGLAMSAKK DAMVQMGGLL CFKDESFLDV YTECRTLCVV
QEGFPTYGGL EGGAMERLAV GLYDGMRQDW LAYRINQVEY LVNGLESIGV VCQQAGGHAA
FVDAGKLLPH IPADQFPAHA LACELYKVAG IRAVEIGSLL LGRDPATGKQ HPCPAELLRL
TIPRATYTQT HMDFIIEAFG KVKANAANVK GLEFTYEPQV LRHFTARLKE IDA