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Protein

Tryptophanase

Gene

tnaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pathwayi: L-tryptophan degradation via pyruvate pathway

This protein is involved in step 1 of the subpathway that synthesizes indole and pyruvate from L-tryptophan.
Proteins known to be involved in this subpathway in this organism are:
  1. Tryptophanase (tnaA)
This subpathway is part of the pathway L-tryptophan degradation via pyruvate pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes indole and pyruvate from L-tryptophan, the pathway L-tryptophan degradation via pyruvate pathway and in Amino-acid degradation.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • L-cysteine desulfhydrase activity Source: EcoCyc
  • potassium ion binding Source: EcoCyc
  • pyridoxal phosphate binding Source: EcoCyc
  • tryptophanase activity Source: EcoCyc

GO - Biological processi

  • tryptophan catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tryptophan catabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:TRYPTOPHAN-MONOMER.
ECOL316407:JW3686-MONOMER.
MetaCyc:TRYPTOPHAN-MONOMER.
BRENDAi4.1.99.1. 2026.
UniPathwayiUPA00332; UER00452.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophanase (EC:4.1.99.1)
Alternative name(s):
L-tryptophan indole-lyase
Short name:
TNase
Gene namesi
Name:tnaA
Synonyms:ind
Ordered Locus Names:b3708, JW3686
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11005. tnaA.

Subcellular locationi

  • Cytoplasm 1 Publication

  • 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.

GO - Cellular componenti

  • cell pole Source: EcoCyc
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Not essential, cells do not produce indole.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi294 – 2941C → S: Identical to wild-type. 1 Publication
Mutagenesisi298 – 2981C → S: Alters activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471TryptophanasePRO_0000195611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6-acetyllysine1 Publication
Modified residuei115 – 1151N6-acetyllysine1 Publication
Modified residuei156 – 1561N6-acetyllysine1 Publication
Modified residuei270 – 2701N6-(pyridoxal phosphate)lysine
Modified residuei450 – 4501N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0A853.
PaxDbiP0A853.
PRIDEiP0A853.

2D gel databases

SWISS-2DPAGEP0A853.

Expressioni

Inductioni

Repressed by cold shock.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-371316,EBI-371316

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262594. 8 interactions.
852523. 1 interaction.
DIPiDIP-31878N.
IntActiP0A853. 12 interactions.
MINTiMINT-1267429.
STRINGi511145.b3708.

Chemistry

BindingDBiP0A853.

Structurei

Secondary structure

1
471
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 189Combined sources
Helixi24 – 3310Combined sources
Turni34 – 363Combined sources
Helixi38 – 403Combined sources
Helixi43 – 453Combined sources
Beta strandi47 – 493Combined sources
Beta strandi53 – 553Combined sources
Helixi61 – 666Combined sources
Helixi67 – 693Combined sources
Beta strandi74 – 763Combined sources
Helixi78 – 9114Combined sources
Beta strandi94 – 996Combined sources
Turni103 – 1053Combined sources
Helixi106 – 12116Combined sources
Turni125 – 1273Combined sources
Beta strandi129 – 1346Combined sources
Helixi137 – 1459Combined sources
Beta strandi149 – 1524Combined sources
Turni156 – 1594Combined sources
Beta strandi161 – 1633Combined sources
Turni166 – 1694Combined sources
Helixi173 – 18311Combined sources
Helixi185 – 1873Combined sources
Beta strandi191 – 1977Combined sources
Helixi199 – 2013Combined sources
Helixi207 – 21913Combined sources
Beta strandi224 – 2274Combined sources
Helixi231 – 24111Combined sources
Helixi243 – 2453Combined sources
Helixi250 – 2578Combined sources
Helixi258 – 2603Combined sources
Beta strandi262 – 2709Combined sources
Beta strandi278 – 2825Combined sources
Helixi285 – 2873Combined sources
Helixi288 – 30013Combined sources
Turni305 – 3095Combined sources
Helixi312 – 32413Combined sources
Helixi328 – 34720Combined sources
Beta strandi352 – 3554Combined sources
Beta strandi360 – 3634Combined sources
Helixi364 – 3674Combined sources
Helixi373 – 3753Combined sources
Helixi377 – 38913Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi394 – 3974Combined sources
Helixi398 – 4014Combined sources
Turni405 – 4073Combined sources
Beta strandi417 – 4204Combined sources
Turni424 – 4263Combined sources
Helixi429 – 44416Combined sources
Helixi446 – 4483Combined sources
Beta strandi452 – 4565Combined sources
Beta strandi459 – 4613Combined sources
Helixi462 – 4654Combined sources
Beta strandi467 – 4704Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C44X-ray2.81A/B/C/D1-471[»]
2OQXX-ray1.90A5-471[»]
2V0YX-ray2.00A5-471[»]
2V1PX-ray1.90A5-471[»]
4UP2X-ray2.78A/B/C/D1-471[»]
4W1YX-ray3.20A/B5-471[»]
4W4HX-ray2.89A/B5-471[»]
5D8GX-ray1.89A5-471[»]
ProteinModelPortaliP0A853.
SMRiP0A853. Positions 4-471.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A853.

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-eliminating lyase family.Curated

Phylogenomic databases

eggNOGiENOG4105C0F. Bacteria.
COG3033. LUCA.
HOGENOMiHOG000057883.
InParanoidiP0A853.
KOiK01667.
OMAiIDACRFA.
PhylomeDBiP0A853.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00544. Tryptophanase. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR011166. Beta-eliminating_lyase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR013440. TNase.
IPR018176. Tryptophanase_CS.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF001386. Trpase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02617. tnaA_trp_ase. 1 hit.
PROSITEiPS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A853-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENFKHLPEP FRIRVIEPVK RTTRAYREEA IIKSGMNPFL LDSEDVFIDL
60 70 80 90 100
LTDSGTGAVT QSMQAAMMRG DEAYSGSRSY YALAESVKNI FGYQYTIPTH
110 120 130 140 150
QGRGAEQIYI PVLIKKREQE KGLDRSKMVA FSNYFFDTTQ GHSQINGCTV
160 170 180 190 200
RNVYIKEAFD TGVRYDFKGN FDLEGLERGI EEVGPNNVPY IVATITSNSA
210 220 230 240 250
GGQPVSLANL KAMYSIAKKY DIPVVMDSAR FAENAYFIKQ REAEYKDWTI
260 270 280 290 300
EQITRETYKY ADMLAMSAKK DAMVPMGGLL CMKDDSFFDV YTECRTLCVV
310 320 330 340 350
QEGFPTYGGL EGGAMERLAV GLYDGMNLDW LAYRIAQVQY LVDGLEEIGV
360 370 380 390 400
VCQQAGGHAA FVDAGKLLPH IPADQFPAQA LACELYKVAG IRAVEIGSFL
410 420 430 440 450
LGRDPKTGKQ LPCPAELLRL TIPRATYTQT HMDFIIEAFK HVKENAANIK
460 470
GLTFTYEPKV LRHFTAKLKE V
Length:471
Mass (Da):52,773
Last modified:June 7, 2005 - v1
Checksum:i5AFC1F41BD9D0034
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1404DTTQ → TTQG no nucleotide entry (PubMed:6268608).Curated
Sequence conflicti379 – 3802QA → TG in AAA24676 (PubMed:6268608).Curated
Sequence conflicti379 – 3802QA → TG in CAA34096 (PubMed:2502187).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE65173. WZEC.
RefSeqiNP_418164.4. NC_000913.3.
WP_001295247.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76731; AAC76731; b3708.
BAE77584; BAE77584; BAE77584.
GeneIDi948221.
KEGGiecj:JW3686.
eco:b3708.
PATRICi32122911. VBIEscCol129921_3831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE65173. WZEC.
RefSeqiNP_418164.4. NC_000913.3.
WP_001295247.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C44X-ray2.81A/B/C/D1-471[»]
2OQXX-ray1.90A5-471[»]
2V0YX-ray2.00A5-471[»]
2V1PX-ray1.90A5-471[»]
4UP2X-ray2.78A/B/C/D1-471[»]
4W1YX-ray3.20A/B5-471[»]
4W4HX-ray2.89A/B5-471[»]
5D8GX-ray1.89A5-471[»]
ProteinModelPortaliP0A853.
SMRiP0A853. Positions 4-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262594. 8 interactions.
852523. 1 interaction.
DIPiDIP-31878N.
IntActiP0A853. 12 interactions.
MINTiMINT-1267429.
STRINGi511145.b3708.

Chemistry

BindingDBiP0A853.

2D gel databases

SWISS-2DPAGEP0A853.

Proteomic databases

EPDiP0A853.
PaxDbiP0A853.
PRIDEiP0A853.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76731; AAC76731; b3708.
BAE77584; BAE77584; BAE77584.
GeneIDi948221.
KEGGiecj:JW3686.
eco:b3708.
PATRICi32122911. VBIEscCol129921_3831.

Organism-specific databases

EchoBASEiEB0998.
EcoGeneiEG11005. tnaA.

Phylogenomic databases

eggNOGiENOG4105C0F. Bacteria.
COG3033. LUCA.
HOGENOMiHOG000057883.
InParanoidiP0A853.
KOiK01667.
OMAiIDACRFA.
PhylomeDBiP0A853.

Enzyme and pathway databases

UniPathwayiUPA00332; UER00452.
BioCyciEcoCyc:TRYPTOPHAN-MONOMER.
ECOL316407:JW3686-MONOMER.
MetaCyc:TRYPTOPHAN-MONOMER.
BRENDAi4.1.99.1. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A853.
PROiP0A853.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00544. Tryptophanase. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR011166. Beta-eliminating_lyase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR013440. TNase.
IPR018176. Tryptophanase_CS.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF001386. Trpase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02617. tnaA_trp_ase. 1 hit.
PROSITEiPS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTNAA_ECOLI
AccessioniPrimary (citable) accession number: P0A853
Secondary accession number(s): P00913, P78123, Q2M822
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: September 7, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.