※ Protein Information
Tag Content
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tryptophanase
Protein Synonyms/Alias
 TNase
Gene Name
 tnaA
Gene Synonyms/Alias
 ind; OrderedLocusNames=b3708, JW3686
Created Date
 3-June-2014
Organism
 Escherichia coli (strain K12)
NCBI Taxa ID
 83333
Phosphorylation
Position
Peptide
Code
Type
References
93 SVKNIFGYQYTIPTH Y HTP [1]
80 AYSGSRSYYALAESV Y HTP [2]
258 EQITRETYKYADMLA Y HTP [2]
386 QALACELYKVAGIRA Y HTP [2]
456 IKGLTFTYEPKVLRH Y HTP [2]
236 ARFAENAYFIKQREA Y HTP [2]
307 VQEGFPTYGGLEGGA Y HTP [2]
165 AFDTGVRYDFKGNFD Y HTP [2]
260 ITRETYKYADMLAMS Y HTP [2]
134 KMVAFSNYFFDTTQG Y HTP [2]
81 YSGSRSYYALAESVK Y HTP [2]
214 LANLKAMYSIAKKYD Y HTP [2]
245 IKQREAEYKDWTIEQ Y HTP [2]
95 KNIFGYQYTIPTHQG Y HTP [2]
Reference
 [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation.
 Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M
 Mol. Cell Proteomics 2008, Feb;7(2):299-307. [PMID:17938405]
 [2]The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence.
 Hansen AM,Chaerkady R,Sharma J,Díaz-Mejía JJ,Tyagi N,Renuse S,Jacob HK,Pinto SM,Sahasrabuddhe NA,Kim MS,Delanghe B,Srinivasan N,Emili A,Kaper JB,Pandey A
 PLoS Pathog. 2013;9(6):e1003403. [PMID:23785281]
Functional Description From UniProt
 
Sequence Annotation From UniProt
 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
Key Word From UniProt
 3D-structure; Acetylation; Completeproteome; Cytoplasm; Directproteinsequencing; Lyase; Pyridoxalphosphate; Referenceproteome; Tryptophancatabolism
Protein Sequence
 MENFKHLPEP FRIRVIEPVK RTTRAYREEA IIKSGMNPFL LDSEDVFIDL LTDSGTGAVT 60
 QSMQAAMMRG DEAYSGSRSY YALAESVKNI FGYQYTIPTH QGRGAEQIYI PVLIKKREQE 120
 KGLDRSKMVA FSNYFFDTTQ GHSQINGCTV RNVYIKEAFD TGVRYDFKGN FDLEGLERGI 180
 EEVGPNNVPY IVATITSNSA GGQPVSLANL KAMYSIAKKY DIPVVMDSAR FAENAYFIKQ 240
 REAEYKDWTI EQITRETYKY ADMLAMSAKK DAMVPMGGLL CMKDDSFFDV YTECRTLCVV 300
 QEGFPTYGGL EGGAMERLAV GLYDGMNLDW LAYRIAQVQY LVDGLEEIGV VCQQAGGHAA 360
 FVDAGKLLPH IPADQFPAQA LACELYKVAG IRAVEIGSFL LGRDPKTGKQ LPCPAELLRL 420
 TIPRATYTQT HMDFIIEAFK HVKENAANIK GLTFTYEPKV LRHFTAKLKE V 471
  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 IPI:IntAct
  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
  GO:0006569   P:tryptophan catabolic process IMP:EcoCyc
  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.
  PF01212   Beta_elim_lyase.
  PS00853   BETA_ELIM_LYASE.