UniProt Accession

 TNAA_ECOLI; P0A853; P00913; P78123; Q2M822 

Genbank Protein ID

 K00032; X15974; M11990; M59914; L10328; U00096; AP009048 

Genbank Nucleotide ID

 AAA24676.1; CAA34096.1; AAA24679.1; AAA62059.1; AAC76731.2; BAE77584.1 

Protein Name

 Tryptophanase 

Protein Synonyms/Alias

 L-tryptophan indole-lyase; TNase 

Gene Name

 tnaA 

Gene Synonyms/Alias

 ind; b3708; JW3686 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
5	***MENFKHLPEPFR	acetylation	[1, 2, 3]
88	YALAESVKNIFGYQY	acetylation	[3]
115	IYIPVLIKKREQEKG	acetylation	[1, 2, 3, 4]
121	IKKREQEKGLDRSKM	acetylation	[3]
127	EKGLDRSKMVAFSNY	acetylation	[3]
156	TVRNVYIKEAFDTGV	acetylation	[1, 2, 3, 4]
156	TVRNVYIKEAFDTGV	pupylation	[5]
168	TGVRYDFKGNFDLEG	acetylation	[3]
211	PVSLANLKAMYSIAK	acetylation	[3]
218	KAMYSIAKKYDIPVV	acetylation	[3]
219	AMYSIAKKYDIPVVM	acetylation	[3]
239	AENAYFIKQREAEYK	acetylation	[2, 3, 4]
246	KQREAEYKDWTIEQI	acetylation	[3, 4]
259	QITRETYKYADMLAM	acetylation	[3, 4]
269	DMLAMSAKKDAMVPM	acetylation	[3]
270	MLAMSAKKDAMVPMG	acetylation	[3]
283	MGGLLCMKDDSFFDV	acetylation	[3]
366	AAFVDAGKLLPHIPA	acetylation	[3]
387	ALACELYKVAGIRAV	acetylation	[3]
406	FLLGRDPKTGKQLPC	acetylation	[4]
409	GRDPKTGKQLPCPAE	acetylation	[3]
440	DFIIEAFKHVKENAA	acetylation	[3]
443	IEAFKHVKENAANIK	acetylation	[3]
450	KENAANIKGLTFTYE	acetylation	[1, 3]
459	LTFTYEPKVLRHFTA	acetylation	[2, 3, 4]

Reference

 [1] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [4] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [5] Reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli.
 Cerda-Maira FA, McAllister F, Bode NJ, Burns KE, Gygi SP, Darwin KH.
 EMBO Rep. 2011 Jul 8;12(8):863-70. [PMID: 21738222] 

Functional Description

  

Sequence Annotation

 MOD_RES 5 5 N6-acetyllysine.
 MOD_RES 115 115 N6-acetyllysine.
 MOD_RES 156 156 N6-acetyllysine.
 MOD_RES 270 270 N6-(pyridoxal phosphate)lysine.
 MOD_RES 450 450 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome; Tryptophan catabolism. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 471 AA 

Protein Sequence

Gene Ontology

 GO:0060187; C:cell pole; IDA:EcoCyc.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0042802; F:identical protein binding; IDA:EcoCyc.
 GO:0080146; F:L-cysteine desulfhydrase activity; IMP:EcoCyc.
 GO:0030955; F:potassium ion binding; IDA:EcoCyc.
 GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
 GO:0009034; F:tryptophanase activity; IDA:EcoCyc. 

Interpro

 IPR001597; 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. 

Pfam

 PF01212; Beta_elim_lyase 

SMART

  

PROSITE

 PS00853; BETA_ELIM_LYASE 

PRINTS