UniProtKB - P0A853 (TNAA_ECOLI)
Protein
Tryptophanase
Gene
tnaA
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalytic activityi
- EC:4.1.99.1
Cofactori
: L-tryptophan degradation via pyruvate pathway Pathwayi
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:
- Tryptophanase (tnaA), Tryptophanase (tnaA)
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
- tryptophan catabolic process Source: EcoCyc
Keywordsi
Molecular function | Lyase |
Biological process | Tryptophan catabolism |
Ligand | Pyridoxal phosphate |
Enzyme and pathway databases
BioCyci | EcoCyc:TRYPTOPHAN-MONOMER MetaCyc:TRYPTOPHAN-MONOMER |
BRENDAi | 4.1.99.1, 2026 |
UniPathwayi | UPA00332;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 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- 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.
Cytosol
- cytosol Source: UniProtKB
Other locations
- cell pole Source: EcoCyc
- membrane Source: UniProtKB
- protein-containing complex Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Disruption phenotypei
Not essential, cells do not produce indole.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 294 | C → S: Identical to wild-type. 1 Publication | 1 | |
Mutagenesisi | 298 | C → S: Alters activity. 1 Publication | 1 |
Miscellaneous databases
PHI-basei | PHI:7966 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000195611 | 1 – 471 | TryptophanaseAdd BLAST | 471 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 5 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 115 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 156 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 270 | N6-(pyridoxal phosphate)lysine | 1 | |
Modified residuei | 450 | N6-acetyllysine1 Publication | 1 |
Keywords - PTMi
AcetylationProteomic databases
jPOSTi | P0A853 |
PaxDbi | P0A853 |
PRIDEi | P0A853 |
2D gel databases
SWISS-2DPAGEi | P0A853 |
PTM databases
iPTMneti | P0A853 |
Expressioni
Inductioni
Repressed by cold shock.1 Publication
Interactioni
Subunit structurei
Homotetramer.
1 PublicationBinary interactionsi
Hide detailsP0A853
With | #Exp. | IntAct |
---|---|---|
dnaK [P0A6Y8] | 2 | EBI-371316,EBI-542092 |
itself | 2 | EBI-371316,EBI-371316 |
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4262594, 19 interactors 852523, 3 interactors |
DIPi | DIP-31878N |
IntActi | P0A853, 13 interactors |
STRINGi | 511145.b3708 |
Chemistry databases
BindingDBi | P0A853 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A853 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A853 |
Family & Domainsi
Sequence similaritiesi
Belongs to the beta-eliminating lyase family.Curated
Phylogenomic databases
eggNOGi | COG3033, Bacteria |
HOGENOMi | CLU_047223_0_0_6 |
InParanoidi | P0A853 |
PhylomeDBi | P0A853 |
Family and domain databases
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
HAMAPi | MF_00544, Tryptophanase, 1 hit |
InterProi | View protein in InterPro IPR001597, ArAA_b-elim_lyase/Thr_aldolase IPR011166, Beta-eliminating_lyase IPR015424, PyrdxlP-dep_Trfase IPR015422, PyrdxlP-dep_Trfase_dom1 IPR015421, PyrdxlP-dep_Trfase_major IPR013440, TNase IPR018176, Tryptophanase_CS |
Pfami | View protein in Pfam PF01212, Beta_elim_lyase, 1 hit |
PIRSFi | PIRSF001386, Trpase, 1 hit |
SUPFAMi | SSF53383, SSF53383, 1 hit |
TIGRFAMsi | TIGR02617, tnaA_trp_ase, 1 hit |
PROSITEi | View protein in PROSITE PS00853, BETA_ELIM_LYASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P0A853-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence AAA62059 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 137 – 140 | DTTQ → TTQG no nucleotide entry (PubMed:6268608).Curated | 4 | |
Sequence conflicti | 379 – 380 | QA → TG in AAA24676 (PubMed:6268608).Curated | 2 | |
Sequence conflicti | 379 – 380 | QA → TG in CAA34096 (PubMed:2502187).Curated | 2 |
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 |
PIRi | E65173, WZEC |
RefSeqi | NP_418164.4, NC_000913.3 WP_001295247.1, NZ_STEB01000015.1 |
Genome annotation databases
EnsemblBacteriai | AAC76731; AAC76731; b3708 BAE77584; BAE77584; BAE77584 |
GeneIDi | 58463277 948221 |
KEGGi | ecj:JW3686 eco:b3708 |
PATRICi | fig|511145.12.peg.3831 |
Similar proteinsi
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 |
PIRi | E65173, WZEC |
RefSeqi | NP_418164.4, NC_000913.3 WP_001295247.1, NZ_STEB01000015.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2C44 | X-ray | 2.81 | A/B/C/D | 1-471 | [»] | |
2OQX | X-ray | 1.90 | A | 5-471 | [»] | |
2V0Y | X-ray | 2.00 | A | 5-471 | [»] | |
2V1P | X-ray | 1.90 | A | 5-471 | [»] | |
4UP2 | X-ray | 2.78 | A/B/C/D | 1-471 | [»] | |
4W1Y | X-ray | 3.20 | A/B | 5-471 | [»] | |
4W4H | X-ray | 2.89 | A/B | 5-471 | [»] | |
5D8G | X-ray | 1.89 | A | 5-471 | [»] | |
SMRi | P0A853 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262594, 19 interactors 852523, 3 interactors |
DIPi | DIP-31878N |
IntActi | P0A853, 13 interactors |
STRINGi | 511145.b3708 |
Chemistry databases
BindingDBi | P0A853 |
PTM databases
iPTMneti | P0A853 |
2D gel databases
SWISS-2DPAGEi | P0A853 |
Proteomic databases
jPOSTi | P0A853 |
PaxDbi | P0A853 |
PRIDEi | P0A853 |
Genome annotation databases
EnsemblBacteriai | AAC76731; AAC76731; b3708 BAE77584; BAE77584; BAE77584 |
GeneIDi | 58463277 948221 |
KEGGi | ecj:JW3686 eco:b3708 |
PATRICi | fig|511145.12.peg.3831 |
Organism-specific databases
EchoBASEi | EB0998 |
Phylogenomic databases
eggNOGi | COG3033, Bacteria |
HOGENOMi | CLU_047223_0_0_6 |
InParanoidi | P0A853 |
PhylomeDBi | P0A853 |
Enzyme and pathway databases
UniPathwayi | UPA00332;UER00452 |
BioCyci | EcoCyc:TRYPTOPHAN-MONOMER MetaCyc:TRYPTOPHAN-MONOMER |
BRENDAi | 4.1.99.1, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0A853 |
PHI-basei | PHI:7966 |
PROi | PR:P0A853 |
Family and domain databases
Gene3Di | 3.40.640.10, 1 hit 3.90.1150.10, 1 hit |
HAMAPi | MF_00544, Tryptophanase, 1 hit |
InterProi | View protein in InterPro IPR001597, ArAA_b-elim_lyase/Thr_aldolase IPR011166, Beta-eliminating_lyase IPR015424, PyrdxlP-dep_Trfase IPR015422, PyrdxlP-dep_Trfase_dom1 IPR015421, PyrdxlP-dep_Trfase_major IPR013440, TNase IPR018176, Tryptophanase_CS |
Pfami | View protein in Pfam PF01212, Beta_elim_lyase, 1 hit |
PIRSFi | PIRSF001386, Trpase, 1 hit |
SUPFAMi | SSF53383, SSF53383, 1 hit |
TIGRFAMsi | TIGR02617, tnaA_trp_ase, 1 hit |
PROSITEi | View protein in PROSITE PS00853, BETA_ELIM_LYASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TNAA_ECOLI | |
Accessioni | P0A853Primary (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: | April 7, 2021 | |
This is version 142 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- 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