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Protein

Tryptophanase

Gene

tnaA

Organism
Proteus vulgaris
Status
Reviewed-Annotation score: Annotation score: 3 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), Tryptophanase (tnaA), Tryptophanase (tnaA), 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

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tryptophan catabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

SABIO-RKP28796.
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
OrganismiProteus vulgaris
Taxonomic identifieri585 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467TryptophanasePRO_0000195619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 169Combined sources
Helixi22 – 3110Combined sources
Helixi36 – 383Combined sources
Helixi41 – 433Combined sources
Beta strandi45 – 473Combined sources
Beta strandi51 – 533Combined sources
Helixi59 – 668Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 8914Combined sources
Beta strandi93 – 997Combined sources
Helixi100 – 11718Combined sources
Beta strandi125 – 1306Combined sources
Helixi133 – 1419Combined sources
Beta strandi145 – 1484Combined sources
Helixi152 – 1554Combined sources
Turni162 – 1654Combined sources
Helixi169 – 17911Combined sources
Helixi181 – 1833Combined sources
Beta strandi184 – 19310Combined sources
Turni194 – 1974Combined sources
Helixi203 – 21614Combined sources
Beta strandi220 – 2234Combined sources
Helixi227 – 23711Combined sources
Helixi239 – 2413Combined sources
Helixi246 – 2538Combined sources
Helixi254 – 2563Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi274 – 2807Combined sources
Helixi282 – 29514Combined sources
Turni299 – 3035Combined sources
Helixi306 – 31813Combined sources
Helixi322 – 34120Combined sources
Beta strandi352 – 3598Combined sources
Turni360 – 3623Combined sources
Helixi368 – 3703Combined sources
Helixi372 – 38413Combined sources
Beta strandi389 – 3924Combined sources
Helixi393 – 3964Combined sources
Turni400 – 4023Combined sources
Beta strandi412 – 4165Combined sources
Helixi424 – 43512Combined sources
Helixi438 – 4414Combined sources
Beta strandi447 – 4515Combined sources
Helixi457 – 4604Combined sources
Beta strandi462 – 4654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AX4X-ray2.10A/B/C/D1-467[»]
ProteinModelPortaliP28796.
SMRiP28796. Positions 2-466.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28796.

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-eliminating lyase family.Curated

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
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.
PROSITEiPS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKRIVEPFR IKMVEKIRVP SREEREAALK EAGYNPFLLP SSAVYIDLLT
60 70 80 90 100
DSGTNAMSDH QWAAMITGDE AYAGSRNYYD LKDKAKELFN YDYIIPAHQG
110 120 130 140 150
RGAENILFPV LLKYKQKEGK AKNPVFISNF HFDTTAAHVE LNGCKAINIV
160 170 180 190 200
TEKAFDSETY DDWKGDFDIK KLKENIAQHG ADNIVAIVST VTCNSAGGQP
210 220 230 240 250
VSMSNLKEVY EIAKQHGIFV VMDSARFCEN AYFIKARDPK YKNATIKEVI
260 270 280 290 300
FDMYKYADAL TMSAKKDPLL NIGGLVAIRD NEEIFTLARQ RCVPMEGFVT
310 320 330 340 350
YGGLAGRDMA AMVQGLEEGT EEEYLHYRIG QVKYLGDRLR EAGIPIQYPT
360 370 380 390 400
GGHAVFVDCK KLVPQIPGDQ FPAQAVINAL YLESGVRAVE IGSFLLGRDP
410 420 430 440 450
ATGEQKHADM EFMRLTIARR VYTNDHMDYI ADALIGLKEK FATLKGLEFE
460
YEPPVLRHFT ARLKPIE
Length:467
Mass (Da):52,490
Last modified:December 1, 1992 - v1
Checksum:iBFDE8E18ED20EF37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93277 Genomic DNA. Translation: AAA25664.1.
PIRiB44038.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93277 Genomic DNA. Translation: AAA25664.1.
PIRiB44038.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AX4X-ray2.10A/B/C/D1-467[»]
ProteinModelPortaliP28796.
SMRiP28796. Positions 2-466.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00332; UER00452.
SABIO-RKP28796.

Miscellaneous databases

EvolutionaryTraceiP28796.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
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.
PROSITEiPS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTNAA_PROVU
AccessioniPrimary (citable) accession number: P28796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 14, 2015
This is version 84 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.