ID A4GWH8_ECO11 Unreviewed; 476 AA.
AC A4GWH8;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Tryptophanase {ECO:0000256|HAMAP-Rule:MF_00544};
DE EC=4.1.99.1 {ECO:0000256|HAMAP-Rule:MF_00544};
DE AltName: Full=L-tryptophan indole-lyase {ECO:0000256|HAMAP-Rule:MF_00544};
DE Short=TNase {ECO:0000256|HAMAP-Rule:MF_00544};
GN Name=tnaA {ECO:0000256|HAMAP-Rule:MF_00544,
GN ECO:0000313|EMBL:ABO32509.1};
OS Escherichia coli O111:H-.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=168927 {ECO:0000313|EMBL:ABO32509.1};
RN [1] {ECO:0000313|EMBL:ABO32509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=O111:H- {ECO:0000313|EMBL:ABO32509.1};
RX PubMed=17693560; DOI=10.1128/AEM.00606-07;
RA Bernasconi C., Volponi G., Picozzi C., Foschino R.;
RT "Use of the tna operon as a new molecular target for Escherichia coli
RT detection.";
RL Appl. Environ. Microbiol. 73:6321-6325(2007).
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:0000256|ARBA:ARBA00001826, ECO:0000256|HAMAP-
CC Rule:MF_00544};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00544, ECO:0000256|PIRSR:PIRSR611166-50};
CC -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC pathway; indole and pyruvate from L-tryptophan: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004662, ECO:0000256|HAMAP-Rule:MF_00544}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00544}.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000256|ARBA:ARBA00009721, ECO:0000256|HAMAP-Rule:MF_00544}.
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DR EMBL; EF445888; ABO32509.1; -; Genomic_DNA.
DR AlphaFoldDB; A4GWH8; -.
DR SMR; A4GWH8; -.
DR UniPathway; UPA00332; UER00452.
DR GO; GO:0009034; F:tryptophanase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR02617; tnaA_trp_ase; 1.
DR PANTHER; PTHR32325; BETA-ELIMINATING LYASE-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32325:SF4; TRYPTOPHANASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF001386; Trpase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|HAMAP-Rule:MF_00544};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00544, ECO:0000313|EMBL:ABO32509.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00544};
KW Tryptophan catabolism {ECO:0000256|ARBA:ARBA00023079, ECO:0000256|HAMAP-
KW Rule:MF_00544}.
FT DOMAIN 54..441
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544"
FT MOD_RES 120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544"
FT MOD_RES 161
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544"
FT MOD_RES 275
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544,
FT ECO:0000256|PIRSR:PIRSR611166-50"
FT MOD_RES 455
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00544"
SQ SEQUENCE 476 AA; 53410 MW; 189E6D7190D64D0A CRC64;
MKDYVMENFK HLPEPFRIRV IEPVKRTTRA YREEAIIKSG MNPFLLDSED VFIDLLTDSG
TGAVTQSMQA AMMRGDEAYS GSRSYYALAE SVKNIFGYQY TIPTHQGRGA EQIYIPVLIK
KREQEKGLDR SKMVAFSNYF FDTTQGHSQI NGCTVRNVYI KEAFDTGVRY DFKGNFDLEG
LERGIEEVGP NNVPYIVATI TSNSAGGQPV SLANLKAMYS IAKKYDIPVV MDSARFAENA
YFIKQREAEY KDWTIEQITR ETYKYADMLA MSAKKDAMVP MGGLLCMKDD SFFDVYTECR
TLCVVQEGFP TYGGLEGGAM ERLAVGLYDG MNLDWLAYRI AQVQYLVDGL EEIGVVCQQA
GGHAAFVDAG KLLPHIPADQ FPAQALACEL YKVAGIRAVE IGSFLLGRDP KTGKQLPCPA
ELLRLTIPRA TYTQTHMDFI IEAFKHVKEN AANIKGLTFT YEPKVLRHFT AKLKEV
//
