TNAA_ECOLI
ID TNAA_ECOLI Reviewed; 471 AA.
AC P0A853; P00913; P78123; Q2M822;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Tryptophanase;
DE EC=4.1.99.1;
DE AltName: Full=L-tryptophan indole-lyase;
DE Short=TNase;
GN Name=tnaA; Synonyms=ind; OrderedLocusNames=b3708, JW3686;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6268608; DOI=10.1128/jb.147.3.787-796.1981;
RA Deeley M.C., Yanofsky C.;
RT "Nucleotide sequence of the structural gene for tryptophanase of
RT Escherichia coli K-12.";
RL J. Bacteriol. 147:787-796(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IMPORTANCE OF CYS-298.
RC STRAIN=B/1t7-A;
RX PubMed=2502187; DOI=10.1016/0300-9084(89)90087-4;
RA Tokushige M., Tsujimoto N., Oda T., Honda T., Yumoto N., Ito S.,
RA Yamamoto M., Kim E.H., Hiragi Y.;
RT "Role of cysteine residues in tryptophanase for monovalent cation-induced
RT activation.";
RL Biochimie 71:711-720(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF TRYPTIC PEPTIDES.
RC STRAIN=K12;
RX PubMed=4551944; DOI=10.1016/s0021-9258(19)45596-8;
RA Kagamiyama H., Matsubara H., Snell E.E.;
RT "The chemical structure of tryptophanase from Escherichia coli. 3.
RT Isolation and amino acid sequence of the tryptic peptides.";
RL J. Biol. Chem. 247:1576-1586(1972).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC STRAIN=K12;
RX PubMed=3902796; DOI=10.1128/jb.164.2.731-740.1985;
RA Stewart V., Yanofsky C.;
RT "Evidence for transcription antitermination control of tryptophanase operon
RT expression in Escherichia coli K-12.";
RL J. Bacteriol. 164:731-740(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 463-471.
RX PubMed=2022620; DOI=10.1128/jb.173.10.3231-3234.1991;
RA Sarsero J.P., Wookey P.J., Gollnick P.D., Yanofsky C., Pittard A.J.;
RT "A new family of integral membrane proteins involved in transport of
RT aromatic amino acids in Escherichia coli.";
RL J. Bacteriol. 173:3231-3234(1991).
RN [9]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [10]
RP PROTEIN SEQUENCE OF 1-8.
RC STRAIN=K12;
RX PubMed=17895580; DOI=10.1266/ggs.82.291;
RA Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
RT "A role of RnlA in the RNase LS activity from Escherichia coli.";
RL Genes Genet. Syst. 82:291-299(2007).
RN [11]
RP MUTAGENESIS OF CYS-294 AND CYS-298.
RX PubMed=2659590; DOI=10.1016/s0021-9258(18)81667-2;
RA Phillips R.S., Gollnick P.D.;
RT "Evidence that cysteine 298 is in the active site of tryptophan indole-
RT lyase.";
RL J. Biol. Chem. 264:10627-10632(1989).
RN [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14527658; DOI=10.1016/s0923-2508(03)00167-0;
RA Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G.,
RA Deho G.;
RT "Changes in Escherichia coli transcriptome during acclimatization at low
RT temperature.";
RL Res. Microbiol. 154:573-580(2003).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-115; LYS-156 AND LYS-450,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [15]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
RA Li G., Young K.D.;
RT "Isolation and identification of new inner membrane-associated proteins
RT that localize to cell poles in Escherichia coli.";
RL Mol. Microbiol. 84:276-295(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP PYRIDOXAL PHOSPHATE, AND PYRIDOXAL PHOSPHATE AT LYS-270.
RX PubMed=16790938; DOI=10.1107/s0907444906019895;
RA Ku S.Y., Yip P., Howell P.L.;
RT "Structure of Escherichia coli tryptophanase.";
RL Acta Crystallogr. D 62:814-823(2006).
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. {ECO:0000269|PubMed:16790938}.
CC -!- INTERACTION:
CC P0A853; P0A6Y8: dnaK; NbExp=2; IntAct=EBI-371316, EBI-542092;
CC P0A853; P0A853: tnaA; NbExp=2; IntAct=EBI-371316, EBI-371316;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22380631}.
CC Note=Almost exclusively localized in foci near 1 cell pole in mid-to-
CC late exponential phase, fewer cells have foci at stationary phase;
CC polar localization depends on the minCDE operon.
CC -!- INDUCTION: Repressed by cold shock. {ECO:0000269|PubMed:14527658}.
CC -!- DISRUPTION PHENOTYPE: Not essential, cells do not produce indole.
CC {ECO:0000269|PubMed:22380631}.
CC -!- SIMILARITY: Belongs to the beta-eliminating lyase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62059.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; K00032; AAA24676.1; -; Genomic_DNA.
DR EMBL; X15974; CAA34096.1; -; Genomic_DNA.
DR EMBL; M11990; AAA24679.1; -; Genomic_DNA.
DR EMBL; M59914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L10328; AAA62059.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76731.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77584.1; -; Genomic_DNA.
DR PIR; E65173; WZEC.
DR RefSeq; NP_418164.4; NC_000913.3.
DR RefSeq; WP_001295247.1; NZ_STEB01000015.1.
DR PDB; 2C44; X-ray; 2.81 A; A/B/C/D=1-471.
DR PDB; 2OQX; X-ray; 1.90 A; A=5-471.
DR PDB; 2V0Y; X-ray; 2.00 A; A=5-471.
DR PDB; 2V1P; X-ray; 1.90 A; A=5-471.
DR PDB; 4UP2; X-ray; 2.78 A; A/B/C/D=1-471.
DR PDB; 4W1Y; X-ray; 3.20 A; A/B=5-471.
DR PDB; 4W4H; X-ray; 2.89 A; A/B=5-471.
DR PDB; 5D8G; X-ray; 1.89 A; A=5-471.
DR PDBsum; 2C44; -.
DR PDBsum; 2OQX; -.
DR PDBsum; 2V0Y; -.
DR PDBsum; 2V1P; -.
DR PDBsum; 4UP2; -.
DR PDBsum; 4W1Y; -.
DR PDBsum; 4W4H; -.
DR PDBsum; 5D8G; -.
DR AlphaFoldDB; P0A853; -.
DR SMR; P0A853; -.
DR BioGRID; 4262594; 19.
DR BioGRID; 852523; 3.
DR DIP; DIP-31878N; -.
DR IntAct; P0A853; 13.
DR STRING; 511145.b3708; -.
DR BindingDB; P0A853; -.
DR iPTMnet; P0A853; -.
DR SWISS-2DPAGE; P0A853; -.
DR jPOST; P0A853; -.
DR PaxDb; P0A853; -.
DR PRIDE; P0A853; -.
DR EnsemblBacteria; AAC76731; AAC76731; b3708.
DR EnsemblBacteria; BAE77584; BAE77584; BAE77584.
DR GeneID; 66672392; -.
DR GeneID; 948221; -.
DR KEGG; ecj:JW3686; -.
DR KEGG; eco:b3708; -.
DR PATRIC; fig|511145.12.peg.3831; -.
DR EchoBASE; EB0998; -.
DR eggNOG; COG3033; Bacteria.
DR HOGENOM; CLU_047223_0_0_6; -.
DR InParanoid; P0A853; -.
DR OMA; EMYQYGD; -.
DR PhylomeDB; P0A853; -.
DR BioCyc; EcoCyc:TRYPTOPHAN-MON; -.
DR BioCyc; MetaCyc:TRYPTOPHAN-MON; -.
DR BRENDA; 4.1.99.1; 2026.
DR UniPathway; UPA00332; UER00452.
DR EvolutionaryTrace; P0A853; -.
DR PHI-base; PHI:7966; -.
DR PRO; PR:P0A853; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0060187; C:cell pole; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc.
DR GO; GO:0030955; F:potassium ion binding; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0009034; F:tryptophanase activity; IDA:EcoCyc.
DR GO; GO:0006569; P:tryptophan catabolic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Lyase;
KW Pyridoxal phosphate; Reference proteome; Tryptophan catabolism.
FT CHAIN 1..471
FT /note="Tryptophanase"
FT /id="PRO_0000195611"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 270
FT /note="N6-(pyridoxal phosphate)lysine"
FT MOD_RES 450
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 294
FT /note="C->S: Identical to wild-type."
FT /evidence="ECO:0000269|PubMed:2659590"
FT MUTAGEN 298
FT /note="C->S: Alters activity."
FT /evidence="ECO:0000269|PubMed:2659590"
FT CONFLICT 137..140
FT /note="DTTQ -> TTQG (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 379..380
FT /note="QA -> TG (in Ref. 1; AAA24676 and 2; CAA34096)"
FT /evidence="ECO:0000305"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:2C44"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:5D8G"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4W4H"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2V0Y"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:5D8G"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2V1P"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:5D8G"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:5D8G"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4W1Y"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:5D8G"
FT TURN 305..309
FT /evidence="ECO:0007829|PDB:2C44"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 328..347
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 377..389
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2C44"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:5D8G"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:5D8G"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 429..444
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:5D8G"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:5D8G"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:5D8G"
SQ SEQUENCE 471 AA; 52773 MW; 5AFC1F41BD9D0034 CRC64;
MENFKHLPEP FRIRVIEPVK RTTRAYREEA IIKSGMNPFL LDSEDVFIDL LTDSGTGAVT
QSMQAAMMRG DEAYSGSRSY YALAESVKNI FGYQYTIPTH QGRGAEQIYI PVLIKKREQE
KGLDRSKMVA FSNYFFDTTQ GHSQINGCTV RNVYIKEAFD TGVRYDFKGN FDLEGLERGI
EEVGPNNVPY IVATITSNSA GGQPVSLANL KAMYSIAKKY DIPVVMDSAR FAENAYFIKQ
REAEYKDWTI EQITRETYKY ADMLAMSAKK DAMVPMGGLL CMKDDSFFDV YTECRTLCVV
QEGFPTYGGL EGGAMERLAV GLYDGMNLDW LAYRIAQVQY LVDGLEEIGV VCQQAGGHAA
FVDAGKLLPH IPADQFPAQA LACELYKVAG IRAVEIGSFL LGRDPKTGKQ LPCPAELLRL
TIPRATYTQT HMDFIIEAFK HVKENAANIK GLTFTYEPKV LRHFTAKLKE V
