TNAA_PROVU
ID TNAA_PROVU Reviewed; 467 AA.
AC P28796;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Tryptophanase;
DE EC=4.1.99.1;
DE AltName: Full=L-tryptophan indole-lyase;
DE Short=TNase;
GN Name=tnaA;
OS Proteus vulgaris.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=585;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400314; DOI=10.1016/s0021-9258(19)88653-2;
RA Kamath A.V., Yanofsky C.;
RT "Characterization of the tryptophanase operon of Proteus vulgaris. Cloning,
RT nucleotide sequence, amino acid homology, and in vitro synthesis of the
RT leader peptide and regulatory analysis.";
RL J. Biol. Chem. 267:19978-19985(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT LYS-266.
RX PubMed=9551100; DOI=10.1006/jmbi.1997.1561;
RA Isupov M.N., Antson A.A., Dodson E.J., Dodson G.G., Dementieva I.S.,
RA Zakomirdina L.N., Wilson K.S., Dauter Z., Lebedev A.A., Harutyunyan E.H.;
RT "Crystal structure of tryptophanase.";
RL J. Mol. Biol. 276:603-623(1998).
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 -!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate
CC pathway; indole and pyruvate from L-tryptophan: step 1/1.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000305}.
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DR EMBL; M93277; AAA25664.1; -; Genomic_DNA.
DR PIR; B44038; B44038.
DR PDB; 1AX4; X-ray; 2.10 A; A/B/C/D=1-467.
DR PDB; 5W19; X-ray; 2.10 A; A/B/C/D=1-467.
DR PDB; 5W1B; X-ray; 2.00 A; A/B/C/D=1-467.
DR PDBsum; 1AX4; -.
DR PDBsum; 5W19; -.
DR PDBsum; 5W1B; -.
DR AlphaFoldDB; P28796; -.
DR SMR; P28796; -.
DR STRING; 585.DR95_2912; -.
DR PRIDE; P28796; -.
DR eggNOG; COG3033; Bacteria.
DR BRENDA; 4.1.99.1; 5049.
DR SABIO-RK; P28796; -.
DR UniPathway; UPA00332; UER00452.
DR EvolutionaryTrace; P28796; -.
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 PROSITE; PS00853; BETA_ELIM_LYASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Pyridoxal phosphate; Tryptophan catabolism.
FT CHAIN 1..467
FT /note="Tryptophanase"
FT /id="PRO_0000195619"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT STRAND 8..16
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:5W1B"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:5W1B"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5W19"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:1AX4"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:5W1B"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:5W1B"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 282..295
FT /evidence="ECO:0007829|PDB:5W1B"
FT TURN 299..303
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 322..341
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:5W1B"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:5W1B"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:5W1B"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:5W19"
FT HELIX 424..435
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5W1B"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:5W1B"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:5W1B"
SQ SEQUENCE 467 AA; 52490 MW; BFDE8E18ED20EF37 CRC64;
MAKRIVEPFR IKMVEKIRVP SREEREAALK EAGYNPFLLP SSAVYIDLLT DSGTNAMSDH
QWAAMITGDE AYAGSRNYYD LKDKAKELFN YDYIIPAHQG RGAENILFPV LLKYKQKEGK
AKNPVFISNF HFDTTAAHVE LNGCKAINIV TEKAFDSETY DDWKGDFDIK KLKENIAQHG
ADNIVAIVST VTCNSAGGQP VSMSNLKEVY EIAKQHGIFV VMDSARFCEN AYFIKARDPK
YKNATIKEVI FDMYKYADAL TMSAKKDPLL NIGGLVAIRD NEEIFTLARQ RCVPMEGFVT
YGGLAGRDMA AMVQGLEEGT EEEYLHYRIG QVKYLGDRLR EAGIPIQYPT GGHAVFVDCK
KLVPQIPGDQ FPAQAVINAL YLESGVRAVE IGSFLLGRDP ATGEQKHADM EFMRLTIARR
VYTNDHMDYI ADALIGLKEK FATLKGLEFE YEPPVLRHFT ARLKPIE
