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

GO - Biological processi

  • cellular amino acid metabolic process Source: InterPro
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi294C → S: Identical to wild-type. 1 Publication1
Mutagenesisi298C → S: Alters activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956111 – 471TryptophanaseAdd BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5N6-acetyllysine1 Publication1
Modified residuei115N6-acetyllysine1 Publication1
Modified residuei156N6-acetyllysine1 Publication1
Modified residuei270N6-(pyridoxal phosphate)lysine1
Modified residuei450N6-acetyllysine1 Publication1

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: EcoCyc

Protein-protein interaction databases

BioGridi4262594. 8 interactors.
852523. 1 interactor.
DIPiDIP-31878N.
IntActiP0A853. 12 interactors.
MINTiMINT-1267429.
STRINGi511145.b3708.

Chemistry databases

BindingDBiP0A853.

Structurei

Secondary structure

1471
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 18Combined sources9
Helixi24 – 33Combined sources10
Turni34 – 36Combined sources3
Helixi38 – 40Combined sources3
Helixi43 – 45Combined sources3
Beta strandi47 – 49Combined sources3
Beta strandi53 – 55Combined sources3
Helixi61 – 66Combined sources6
Helixi67 – 69Combined sources3
Beta strandi74 – 76Combined sources3
Helixi78 – 91Combined sources14
Beta strandi94 – 99Combined sources6
Turni103 – 105Combined sources3
Helixi106 – 121Combined sources16
Turni125 – 127Combined sources3
Beta strandi129 – 134Combined sources6
Helixi137 – 145Combined sources9
Beta strandi149 – 152Combined sources4
Turni156 – 159Combined sources4
Beta strandi161 – 163Combined sources3
Turni166 – 169Combined sources4
Helixi173 – 183Combined sources11
Helixi185 – 187Combined sources3
Beta strandi191 – 197Combined sources7
Helixi199 – 201Combined sources3
Helixi207 – 219Combined sources13
Beta strandi224 – 227Combined sources4
Helixi231 – 241Combined sources11
Helixi243 – 245Combined sources3
Helixi250 – 257Combined sources8
Helixi258 – 260Combined sources3
Beta strandi262 – 270Combined sources9
Beta strandi278 – 282Combined sources5
Helixi285 – 287Combined sources3
Helixi288 – 300Combined sources13
Turni305 – 309Combined sources5
Helixi312 – 324Combined sources13
Helixi328 – 347Combined sources20
Beta strandi352 – 355Combined sources4
Beta strandi360 – 363Combined sources4
Helixi364 – 367Combined sources4
Helixi373 – 375Combined sources3
Helixi377 – 389Combined sources13
Beta strandi390 – 392Combined sources3
Beta strandi394 – 397Combined sources4
Helixi398 – 401Combined sources4
Turni405 – 407Combined sources3
Beta strandi417 – 420Combined sources4
Turni424 – 426Combined sources3
Helixi429 – 444Combined sources16
Helixi446 – 448Combined sources3
Beta strandi452 – 456Combined sources5
Beta strandi459 – 461Combined sources3
Helixi462 – 465Combined sources4
Beta strandi467 – 470Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti137 – 140DTTQ → TTQG no nucleotide entry (PubMed:6268608).Curated4
Sequence conflicti379 – 380QA → TG in AAA24676 (PubMed:6268608).Curated2
Sequence conflicti379 – 380QA → TG in CAA34096 (PubMed:2502187).Curated2

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262594. 8 interactors.
852523. 1 interactor.
DIPiDIP-31878N.
IntActiP0A853. 12 interactors.
MINTiMINT-1267429.
STRINGi511145.b3708.

Chemistry databases

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: November 2, 2016
This is version 111 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.