TNAA_PHOLL
ID TNAA_PHOLL Reviewed; 466 AA.
AC Q7N8C9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=plu0799;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(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; BX571861; CAE13094.1; -; Genomic_DNA.
DR RefSeq; WP_011145173.1; NC_005126.1.
DR AlphaFoldDB; Q7N8C9; -.
DR SMR; Q7N8C9; -.
DR STRING; 243265.plu0799; -.
DR EnsemblBacteria; CAE13094; CAE13094; plu0799.
DR GeneID; 24167848; -.
DR KEGG; plu:plu0799; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_6; -.
DR OMA; EMYQYGD; -.
DR OrthoDB; 91973at2; -.
DR BioCyc; PLUM243265:PLU_RS03980-MON; -.
DR UniPathway; UPA00332; UER00452.
DR Proteomes; UP000002514; 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 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..466
FT /note="Tryptophanase"
FT /id="PRO_0000195617"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00544"
SQ SEQUENCE 466 AA; 52277 MW; DB438738121BDD35 CRC64;
MKRIPEPFRI KMVENIRMTT RAEREKALEE AGYNPFLLPS DAVYIDLLTD SGTGAMSDRQ
WAGIMMGDEA YAGSRNYYHL CDKVNELIGY QYTIPTHQGR GAEQILFPTL IARKKAQGGA
THPVFISNFH FDTTAAHVEL NGAKAINVVT SKAFDTTTYY DWKGDFDIDE LEKTIAEHGA
DNVVAIITTV TCNSSGGQPI SLANMKAVYE IAKQHDIPVV IDSARFCENA WFIKQREKGY
ENKSVKQIVK EMYQYGDMLT MSAKKDPLVN IGGLCCFRDD EDLFNEVRTR CVPMEGFVTY
GGLAGRDMEA LAIGLEEGMN EGYLAYRINQ VAYLGNRLRD AGIPIQYPTG GHAVFVDAKL
LLPHIPGEQF PAHALNNELY LEAGIRSVEI GSLLLGRDPK TGKQKPSPME LLRLTIPRRV
YTNDHMDYVV EAFISLKERI PQIKGLTFTY EPSVLRHFVA RLKPIK