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P0A853 (TNAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophanase

EC=4.1.99.1
Alternative name(s):
L-tryptophan indole-lyase
Short name=TNase
Gene names
Name:tnaA
Synonyms:ind
Ordered Locus Names:b3708, JW3686
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-tryptophan + H2O = indole + pyruvate + NH3. HAMAP MF_00544

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid degradation; L-tryptophan degradation via pyruvate pathway; indole and pyruvate from L-tryptophan: step 1/1. HAMAP MF_00544

Subunit structure

Homotetramer.

Induction

Repressed by cold shock. Ref.11

Sequence similarities

Belongs to the beta-eliminating lyase family.

Sequence caution

The sequence AAA62059.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Tryptophanase HAMAP MF_00544
PRO_0000195611

Amino acid modifications

Modified residue51N6-acetyllysine Ref.12
Modified residue1151N6-acetyllysine Ref.12
Modified residue1561N6-acetyllysine Ref.12
Modified residue2701N6-(pyridoxal phosphate)lysine HAMAP MF_00544
Modified residue4501N6-acetyllysine Ref.12

Experimental info

Mutagenesis2941C → S: Identical to wild-type. Ref.10
Mutagenesis2981C → S: Alters activity. Ref.10
Sequence conflict137 – 1404DTTQ → TTQG no nucleotide entry Ref.1
Sequence conflict379 – 3802QA → TG in AAA24676. Ref.1
Sequence conflict379 – 3802QA → TG in CAA34096. Ref.2

Secondary structure

......................................................................................... 471
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A853 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 5AFC1F41BD9D0034

FASTA47152,773
        10         20         30         40         50         60 
MENFKHLPEP FRIRVIEPVK RTTRAYREEA IIKSGMNPFL LDSEDVFIDL LTDSGTGAVT 

        70         80         90        100        110        120 
QSMQAAMMRG DEAYSGSRSY YALAESVKNI FGYQYTIPTH QGRGAEQIYI PVLIKKREQE 

       130        140        150        160        170        180 
KGLDRSKMVA FSNYFFDTTQ GHSQINGCTV RNVYIKEAFD TGVRYDFKGN FDLEGLERGI 

       190        200        210        220        230        240 
EEVGPNNVPY IVATITSNSA GGQPVSLANL KAMYSIAKKY DIPVVMDSAR FAENAYFIKQ 

       250        260        270        280        290        300 
REAEYKDWTI EQITRETYKY ADMLAMSAKK DAMVPMGGLL CMKDDSFFDV YTECRTLCVV 

       310        320        330        340        350        360 
QEGFPTYGGL EGGAMERLAV GLYDGMNLDW LAYRIAQVQY LVDGLEEIGV VCQQAGGHAA 

       370        380        390        400        410        420 
FVDAGKLLPH IPADQFPAQA LACELYKVAG IRAVEIGSFL LGRDPKTGKQ LPCPAELLRL 

       430        440        450        460        470 
TIPRATYTQT HMDFIIEAFK HVKENAANIK GLTFTYEPKV LRHFTAKLKE V 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12."
Deeley M.C., Yanofsky C.
J. Bacteriol. 147:787-796(1981) [PubMed: 6268608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Role of cysteine residues in tryptophanase for monovalent cation-induced activation."
Tokushige M., Tsujimoto N., Oda T., Honda T., Yumoto N., Ito S., Yamamoto M., Kim E.H., Hiragi Y.
Biochimie 71:711-720(1989) [PubMed: 2502187] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IMPORTANCE OF CYS-298.
Strain: B/1t7-A.
[3]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed: 7686882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The chemical structure of tryptophanase from Escherichia coli. 3. Isolation and amino acid sequence of the tryptic peptides."
Kagamiyama H., Matsubara H., Snell E.E.
J. Biol. Chem. 247:1576-1586(1972) [PubMed: 4551944] [Abstract]
Cited for: PROTEIN SEQUENCE OF TRYPTIC PEPTIDES.
Strain: K12.
[7]"Evidence for transcription antitermination control of tryptophanase operon expression in Escherichia coli K-12."
Stewart V., Yanofsky C.
J. Bacteriol. 164:731-740(1985) [PubMed: 3902796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
Strain: K12.
[8]"A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli."
Sarsero J.P., Wookey P.J., Gollnick P.D., Yanofsky C., Pittard A.J.
J. Bacteriol. 173:3231-3234(1991) [PubMed: 2022620] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 463-471.
[9]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[10]"Evidence that cysteine 298 is in the active site of tryptophan indole-lyase."
Phillips R.S., Gollnick P.D.
J. Biol. Chem. 264:10627-10632(1989) [PubMed: 2659590] [Abstract]
Cited for: MUTAGENESIS OF CYS-294 AND CYS-298.
[11]"Changes in Escherichia coli transcriptome during acclimatization at low temperature."
Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G., Deho G.
Res. Microbiol. 154:573-580(2003) [PubMed: 14527658] [Abstract]
Cited for: INDUCTION.
Strain: K12 / MG1655 / ATCC 47076.
[12]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-115; LYS-156 AND LYS-450, MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[13]"Structure of Escherichia coli tryptophanase."
Ku S.Y., Yip P., Howell P.L.
Acta Crystallogr. D 62:814-823(2006) [PubMed: 16790938] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH PYRIDOXAL PHOSPHATE, PYRIDOXAL PHOSPHATE AT LYS-270.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K00032 Genomic DNA. Translation: AAA24676.1.
X15974 Genomic DNA. Translation: CAA34096.1.
M11990 Genomic DNA. Translation: AAA24679.1.
M59914 Genomic DNA. No translation available.
L10328 Genomic DNA. Translation: AAA62059.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76731.2.
AP009048 Genomic DNA. Translation: BAE77584.1.
PIRWZEC. E65173.
RefSeqNP_418164.4. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C44X-ray2.81A/B/C/D1-471[»]
2OQXX-ray1.90A5-471[»]
2V0YX-ray2.00A5-471[»]
2V1PX-ray1.90A5-471[»]
ProteinModelPortalP0A853.
SMRP0A853. Positions 4-471.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31878N.
IntActP0A853. 12 interactions.
MINTMINT-1267429.

PTM databases

PhosSiteP0A853.

2D gel databases

SWISS-2DPAGEP0A853.
ECO2DBASEG046.5. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000004574; EBESCP00000004574; EBESCG00000003734.
EBESCT00000015295; EBESCP00000014586; EBESCG00000014355.
GeneID948221.
GenomeReviewsGene locus JW3686 in contig AP009048_GR.
Gene locus b3708 in contig U00096_GR.
KEGGecj:JW3686.
eco:b3708.
PATRIC32122911. VBIEscCol129921_3831.

Organism-specific databases

EchoBASEEB0998.
EcoGeneEG11005. tnaA.

Phylogenomic databases

eggNOGCOG3033.
GeneTreeEBGT00050000011364.
HOGENOMHBG297784.
OMAIYFSARK.
PhylomeDBP0A853.
ProtClustDBPRK13238.

Enzyme and pathway databases

BioCycEcoCyc:TRYPTOPHAN-MONOMER.
MetaCyc:TRYPTOPHAN-MONOMER.

Gene expression databases

GenevestigatorP0A853.

Family and domain databases

HAMAPMF_00544. Tryptophanase.
[Tree]
InterProIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR011166. Beta-eliminating_lyase.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR013440. TNase.
IPR018176. Tryptophanase_CS.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK01667.
PfamPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFPIRSF001386. Trpase. 1 hit.
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR02617. TnaA_trp_ase. 1 hit.
PROSITEPS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTNAA_ECOLI
AccessionPrimary (citable) accession number: P0A853
Secondary accession number(s): P00913, P78123, Q2M822
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families