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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: TNAA_ECOLI




SWISS-2DPAGE:  TNAA_ECOLI


TNAA_ECOLI


General information about the entry
View entry in simple text format
Entry nameTNAA_ECOLI
Primary accession numberP0A853
Secondary accession number(s) P00913
integrated into SWISS-2DPAGE on May 15, 2003 (release 16)
2D Annotations were last modified onMarch 31, 2004 (version 1)
General Annotations were last modified on May 19, 2011 (version 7)
Name and origin of the protein
DescriptionRecName: Full=Tryptophanase; EC=4.1.99.1; AltName: Full=L-tryptophan indole-lyase; Short=TNase;.
Gene nameName=tnaA
Synonyms=ind
OrderedLocusNames=b3708, JW3686
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   MAPPING ON GEL
PubMed=12469338; [NCBI, ExPASy, EBI, Israel, Japan]
Yan J.X., Devenish A.T., Wait R., Stone T., Lewis S., Fowler S.
''''''Fluorescence 2-D difference gel electrophoresis and mass spectrometry based proteomic analysis of E. coli'';'';''
Proteomics 2(1):1682-1698(2002)
Comments
  • SUBUNIT: Homotetramer
2D PAGE maps for identified proteins
How to interpret a protein

ECOLI-DIGE4.5-6.5 {Escherichia coli DIGE (4.5-6.5)}
Escherichia coli
ECOLI-DIGE4.5-6.5
  map experimental info
  protein estimated location
 
ECOLI-DIGE4.5-6.5

MAP LOCATIONS:
pI=5.81; Mw=48395  [identification data]

EXPRESSION:
decrease after benzoic acid treatment [1].

MAPPING (identification):
Tandem mass spectrometry [1].

Copyright
This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://world-2dpage.expasy.org/swiss-2dpage/docs/license.html or send email from license@isb-sib.ch).
Cross-references
ECO2DBASEG046.5; 6TH EDITION.
UniProtKB/Swiss-ProtP0A853; TNAA_ECOLI.
2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_10
Entry nameTNAA_ECOLI
Primary accession numberP0A853
Secondary accession number(s) P00913 P78123 Q2M822
Sequence was last modified on June 7, 2005 (version 1)
Annotations were last modified on October 19, 2011 (version 67)
Name and origin of the protein
DescriptionRecName: Full=Tryptophanase; EC=4.1.99.1; AltName: Full=L-tryptophan indole-lyase; Short=TNase;
Gene nameName=tnaA
Synonyms=ind
OrderedLocusNames=b3708, JW3686
Encoded onName=tnaA; Synonyms=ind; OrderedLocusNames=b3708, JW3686
Keywords3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome; Tryptophan catabolism.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLK00032; AAA24676.1; -; Genomic_DNA
EMBLX15974; CAA34096.1; -; Genomic_DNA
EMBLM11990; AAA24679.1; -; Genomic_DNA
EMBLM59914; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLL10328; AAA62059.1; ALT_INIT; Genomic_DNA
EMBLU00096; AAC76731.2; -; Genomic_DNA
EMBLAP009048; BAE77584.1; -; Genomic_DNA
PIRE65173; WZEC; .
RefSeqNP_418164.4; NC_000913.2; .
PDB2C44; X-ray; 2.81 A; A/B/C/D=1-471
PDB2OQX; X-ray; 1.90 A; A=5-471
PDB2V0Y; X-ray; 2.00 A; A=5-471
PDB2V1P; X-ray; 1.90 A; A=5-471
PDBsum2C44; -; .
PDBsum2OQX; -; .
PDBsum2V0Y; -; .
PDBsum2V1P; -; .
ProteinModelPortalP0A853; -; .
SMRP0A853; 4-471; .
DIPDIP-31878N; -; .
IntActP0A853; 10; .
MINTMINT-1267429; -; .
PhosSiteP0A853; -; .
SWISS-2DPAGEP0A853; -; .
ECO2DBASEG046.5; 6TH EDITION; .
EnsemblBacteriaEBESCT00000004574; EBESCP00000004574; EBESCG00000003734; .
EnsemblBacteriaEBESCT00000015295; EBESCP00000014586; EBESCG00000014355; .
GeneID948221; -; .
GenomeReviewsAP009048_GR; JW3686; .
GenomeReviewsU00096_GR; b3708; .
KEGGecj:JW3686; -; .
KEGGeco:b3708; -; .
EchoBASEEB0998; -; .
EcoGeneEG11005; tnaA; .
eggNOGCOG3033; -; .
GeneTreeEBGT00050000011364; -; .
HOGENOMHBG297784; -; .
OMAIYFSARK; -; .
ProtClustDBPRK13238; -; .
BioCycEcoCyc:TRYPTOPHAN-MONOMER; -; .
BioCycMetaCyc:TRYPTOPHAN-MONOMER; -; .
GenevestigatorP0A853; -; .
GOGO:0005829; C:cytosol; IDA:UniProtKB; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc; .
GOGO:0030170; F:pyridoxal phosphate binding; EXP:EcoCyc; .
GOGO:0009034; F:tryptophanase activity; IDA:EcoCyc; .
GOGO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-KW; .
HAMAPMF_00544; Tryptophanase; 1; -
InterProIPR001597; ArAA_b-elim_lyase/Thr_aldolase; .
InterProIPR015424; PyrdxlP-dep_Trfase_major_dom; .
InterProIPR015421; PyrdxlP-dep_Trfase_major_sub1; .
InterProIPR015422; PyrdxlP-dep_Trfase_major_sub2; .
InterProIPR011166; TNase; .
InterProIPR013440; TNase_proteobac; .
InterProIPR018176; Tryptophanase_CS; .
Gene3DG3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1; .
Gene3DG3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 2; .
PfamPF01212; Beta_elim_lyase; 1; .
PIRSFPIRSF001386; Trpase; 1; .
SUPFAMSSF53383; PyrdxlP-dep_Trfase_major; 1; .
TIGRFAMsTIGR02617; TnaA_trp_ase; 1; .
PROSITEPS00853; BETA_ELIM_LYASE; 1; .



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Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server