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Tryptophanase (EC 4.1.99.1) (L-tryptophan indole-lyase) (TNase)

 TNAA_ECOLI              Reviewed;         471 AA.
P0A853; P00913; P78123; Q2M822;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 1.
25-OCT-2017, entry version 120.
RecName: Full=Tryptophanase;
EC=4.1.99.1;
AltName: Full=L-tryptophan indole-lyase;
Short=TNase;
Name=tnaA; Synonyms=ind; OrderedLocusNames=b3708, JW3686;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=6268608;
Deeley M.C., Yanofsky C.;
"Nucleotide sequence of the structural gene for tryptophanase of
Escherichia coli K-12.";
J. Bacteriol. 147:787-796(1981).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IMPORTANCE OF CYS-298.
STRAIN=B/1t7-A;
PubMed=2502187; DOI=10.1016/0300-9084(89)90087-4;
Tokushige M., Tsujimoto N., Oda T., Honda T., Yumoto N., Ito S.,
Yamamoto M., Kim E.H., Hiragi Y.;
"Role of cysteine residues in tryptophanase for monovalent cation-
induced activation.";
Biochimie 71:711-720(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7686882; DOI=10.1006/geno.1993.1230;
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
"DNA sequence and analysis of 136 kilobases of the Escherichia coli
genome: organizational symmetry around the origin of replication.";
Genomics 16:551-561(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF TRYPTIC PEPTIDES.
STRAIN=K12;
PubMed=4551944;
Kagamiyama H., Matsubara H., Snell E.E.;
"The chemical structure of tryptophanase from Escherichia coli. 3.
Isolation and amino acid sequence of the tryptic peptides.";
J. Biol. Chem. 247:1576-1586(1972).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
STRAIN=K12;
PubMed=3902796;
Stewart V., Yanofsky C.;
"Evidence for transcription antitermination control of tryptophanase
operon expression in Escherichia coli K-12.";
J. Bacteriol. 164:731-740(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 463-471.
PubMed=2022620; DOI=10.1128/jb.173.10.3231-3234.1991;
Sarsero J.P., Wookey P.J., Gollnick P.D., Yanofsky C., Pittard A.J.;
"A new family of integral membrane proteins involved in transport of
aromatic amino acids in Escherichia coli.";
J. Bacteriol. 173:3231-3234(1991).
[9]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[10]
PROTEIN SEQUENCE OF 1-8.
STRAIN=K12;
PubMed=17895580; DOI=10.1266/ggs.82.291;
Otsuka Y., Koga M., Iwamoto A., Yonesaki T.;
"A role of RnlA in the RNase LS activity from Escherichia coli.";
Genes Genet. Syst. 82:291-299(2007).
[11]
MUTAGENESIS OF CYS-294 AND CYS-298.
PubMed=2659590;
Phillips R.S., Gollnick P.D.;
"Evidence that cysteine 298 is in the active site of tryptophan
indole-lyase.";
J. Biol. Chem. 264:10627-10632(1989).
[12]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[13]
INDUCTION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=14527658; DOI=10.1016/S0923-2508(03)00167-0;
Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V.,
Pesole G., Deho G.;
"Changes in Escherichia coli transcriptome during acclimatization at
low temperature.";
Res. Microbiol. 154:573-580(2003).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-115; LYS-156 AND
LYS-450, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[15]
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
Li G., Young K.D.;
"Isolation and identification of new inner membrane-associated
proteins that localize to cell poles in Escherichia coli.";
Mol. Microbiol. 84:276-295(2012).
[16]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX
WITH PYRIDOXAL PHOSPHATE, AND PYRIDOXAL PHOSPHATE AT LYS-270.
PubMed=16790938; DOI=10.1107/S0907444906019895;
Ku S.Y., Yip P., Howell P.L.;
"Structure of Escherichia coli tryptophanase.";
Acta Crystallogr. D 62:814-823(2006).
-!- CATALYTIC ACTIVITY: L-tryptophan + H(2)O = indole + pyruvate +
NH(3).
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- PATHWAY: Amino-acid degradation; L-tryptophan degradation via
pyruvate pathway; indole and pyruvate from L-tryptophan: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16790938}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-371316, EBI-371316;
P0A6Y8:dnaK; NbExp=2; IntAct=EBI-371316, EBI-542092;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22380631}.
Note=Almost exclusively localized in foci near 1 cell pole in mid-
to-late exponential phase, fewer cells have foci at stationary
phase; polar localization depends on the minCDE operon.
-!- INDUCTION: Repressed by cold shock. {ECO:0000269|PubMed:14527658}.
-!- DISRUPTION PHENOTYPE: Not essential, cells do not produce indole.
{ECO:0000269|PubMed:22380631}.
-!- SIMILARITY: Belongs to the beta-eliminating lyase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA62059.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; K00032; AAA24676.1; -; Genomic_DNA.
EMBL; X15974; CAA34096.1; -; Genomic_DNA.
EMBL; M11990; AAA24679.1; -; Genomic_DNA.
EMBL; M59914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L10328; AAA62059.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC76731.2; -; Genomic_DNA.
EMBL; AP009048; BAE77584.1; -; Genomic_DNA.
PIR; E65173; WZEC.
RefSeq; NP_418164.4; NC_000913.3.
RefSeq; WP_001295247.1; NZ_LN832404.1.
PDB; 2C44; X-ray; 2.81 A; A/B/C/D=1-471.
PDB; 2OQX; X-ray; 1.90 A; A=5-471.
PDB; 2V0Y; X-ray; 2.00 A; A=5-471.
PDB; 2V1P; X-ray; 1.90 A; A=5-471.
PDB; 4UP2; X-ray; 2.78 A; A/B/C/D=1-471.
PDB; 4W1Y; X-ray; 3.20 A; A/B=5-471.
PDB; 4W4H; X-ray; 2.89 A; A/B=5-471.
PDB; 5D8G; X-ray; 1.89 A; A=5-471.
PDBsum; 2C44; -.
PDBsum; 2OQX; -.
PDBsum; 2V0Y; -.
PDBsum; 2V1P; -.
PDBsum; 4UP2; -.
PDBsum; 4W1Y; -.
PDBsum; 4W4H; -.
PDBsum; 5D8G; -.
ProteinModelPortal; P0A853; -.
SMR; P0A853; -.
BioGrid; 4262594; 8.
BioGrid; 852523; 1.
DIP; DIP-31878N; -.
IntAct; P0A853; 13.
MINT; MINT-1267429; -.
STRING; 316385.ECDH10B_3895; -.
BindingDB; P0A853; -.
iPTMnet; P0A853; -.
SWISS-2DPAGE; P0A853; -.
PaxDb; P0A853; -.
PRIDE; P0A853; -.
EnsemblBacteria; AAC76731; AAC76731; b3708.
EnsemblBacteria; BAE77584; BAE77584; BAE77584.
GeneID; 948221; -.
KEGG; ecj:JW3686; -.
KEGG; eco:b3708; -.
PATRIC; fig|511145.12.peg.3831; -.
EchoBASE; EB0998; -.
EcoGene; EG11005; tnaA.
eggNOG; ENOG4105C0F; Bacteria.
eggNOG; COG3033; LUCA.
HOGENOM; HOG000057883; -.
InParanoid; P0A853; -.
KO; K01667; -.
PhylomeDB; P0A853; -.
BioCyc; EcoCyc:TRYPTOPHAN-MONOMER; -.
BioCyc; MetaCyc:TRYPTOPHAN-MONOMER; -.
BRENDA; 4.1.99.1; 2026.
UniPathway; UPA00332; UER00452.
EvolutionaryTrace; P0A853; -.
PRO; PR:P0A853; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0060187; C:cell pole; IDA:EcoCyc.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc.
GO; GO:0030955; F:potassium ion binding; IDA:EcoCyc.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
GO; GO:0009034; F:tryptophanase activity; IDA:EcoCyc.
GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
GO; GO:0006569; P:tryptophan catabolic process; IMP:EcoCyc.
Gene3D; 3.90.1150.10; -; 2.
HAMAP; MF_00544; Tryptophanase; 1.
InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
InterPro; IPR011166; Beta-eliminating_lyase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
InterPro; IPR013440; TNase.
InterPro; IPR018176; Tryptophanase_CS.
Pfam; PF01212; Beta_elim_lyase; 1.
PIRSF; PIRSF001386; Trpase; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR02617; tnaA_trp_ase; 1.
PROSITE; PS00853; BETA_ELIM_LYASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Lyase; Pyridoxal phosphate;
Reference proteome; Tryptophan catabolism.
CHAIN 1 471 Tryptophanase.
/FTId=PRO_0000195611.
MOD_RES 5 5 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 115 115 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 156 156 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 270 270 N6-(pyridoxal phosphate)lysine.
MOD_RES 450 450 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MUTAGEN 294 294 C->S: Identical to wild-type.
{ECO:0000269|PubMed:2659590}.
MUTAGEN 298 298 C->S: Alters activity.
{ECO:0000269|PubMed:2659590}.
CONFLICT 137 140 DTTQ -> TTQG (in Ref. 1; no nucleotide
entry). {ECO:0000305}.
CONFLICT 379 380 QA -> TG (in Ref. 1; AAA24676 and 2;
CAA34096). {ECO:0000305}.
STRAND 10 18 {ECO:0000244|PDB:2C44}.
HELIX 24 33 {ECO:0000244|PDB:5D8G}.
TURN 34 36 {ECO:0000244|PDB:5D8G}.
HELIX 38 40 {ECO:0000244|PDB:5D8G}.
HELIX 43 45 {ECO:0000244|PDB:5D8G}.
STRAND 47 49 {ECO:0000244|PDB:5D8G}.
STRAND 53 55 {ECO:0000244|PDB:4W4H}.
HELIX 61 66 {ECO:0000244|PDB:5D8G}.
HELIX 67 69 {ECO:0000244|PDB:2V0Y}.
STRAND 74 76 {ECO:0000244|PDB:5D8G}.
HELIX 78 91 {ECO:0000244|PDB:5D8G}.
STRAND 94 99 {ECO:0000244|PDB:5D8G}.
TURN 103 105 {ECO:0000244|PDB:2V1P}.
HELIX 106 121 {ECO:0000244|PDB:5D8G}.
TURN 125 127 {ECO:0000244|PDB:5D8G}.
STRAND 129 134 {ECO:0000244|PDB:5D8G}.
HELIX 137 145 {ECO:0000244|PDB:5D8G}.
STRAND 149 152 {ECO:0000244|PDB:5D8G}.
TURN 156 159 {ECO:0000244|PDB:5D8G}.
STRAND 161 163 {ECO:0000244|PDB:4W1Y}.
TURN 166 169 {ECO:0000244|PDB:5D8G}.
HELIX 173 183 {ECO:0000244|PDB:5D8G}.
HELIX 185 187 {ECO:0000244|PDB:5D8G}.
STRAND 191 197 {ECO:0000244|PDB:5D8G}.
HELIX 199 201 {ECO:0000244|PDB:5D8G}.
HELIX 207 219 {ECO:0000244|PDB:5D8G}.
STRAND 224 227 {ECO:0000244|PDB:5D8G}.
HELIX 231 241 {ECO:0000244|PDB:5D8G}.
HELIX 243 245 {ECO:0000244|PDB:5D8G}.
HELIX 250 257 {ECO:0000244|PDB:5D8G}.
HELIX 258 260 {ECO:0000244|PDB:5D8G}.
STRAND 262 270 {ECO:0000244|PDB:5D8G}.
STRAND 278 282 {ECO:0000244|PDB:5D8G}.
HELIX 285 287 {ECO:0000244|PDB:5D8G}.
HELIX 288 300 {ECO:0000244|PDB:5D8G}.
TURN 305 309 {ECO:0000244|PDB:2C44}.
HELIX 312 324 {ECO:0000244|PDB:5D8G}.
HELIX 328 347 {ECO:0000244|PDB:5D8G}.
STRAND 352 355 {ECO:0000244|PDB:5D8G}.
STRAND 360 363 {ECO:0000244|PDB:5D8G}.
HELIX 364 367 {ECO:0000244|PDB:5D8G}.
HELIX 373 375 {ECO:0000244|PDB:5D8G}.
HELIX 377 389 {ECO:0000244|PDB:5D8G}.
STRAND 390 392 {ECO:0000244|PDB:2C44}.
STRAND 394 397 {ECO:0000244|PDB:5D8G}.
HELIX 398 401 {ECO:0000244|PDB:5D8G}.
TURN 405 407 {ECO:0000244|PDB:5D8G}.
STRAND 417 420 {ECO:0000244|PDB:5D8G}.
TURN 424 426 {ECO:0000244|PDB:5D8G}.
HELIX 429 444 {ECO:0000244|PDB:5D8G}.
HELIX 446 448 {ECO:0000244|PDB:5D8G}.
STRAND 452 456 {ECO:0000244|PDB:5D8G}.
STRAND 459 461 {ECO:0000244|PDB:5D8G}.
HELIX 462 465 {ECO:0000244|PDB:5D8G}.
STRAND 467 470 {ECO:0000244|PDB:5D8G}.
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


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