P0A853 (TNAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophanase
EC=4.1.99.1

Alternative name(s):
L-tryptophan indole-lyase
Short name=TNase

Gene names

Name:	tnaA
Synonyms:	ind
Ordered Locus Names:	b3708, JW3686

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-tryptophan + H2O = indole + pyruvate + NH3. HAMAP-Rule MF_00544
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid degradation; L-tryptophan degradation via pyruvate pathway; indole and pyruvate from L-tryptophan: step 1/1. HAMAP-Rule MF_00544
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm Probable. 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. Ref.15
Induction	Repressed by cold shock. Ref.13
Disruption phenotype	Not essential, cells do not produce indole. Ref.15
Sequence similarities	Belongs to the beta-eliminating lyase family.
Sequence caution	The sequence AAA62059.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Tryptophan catabolism
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cell pole Inferred from direct assay Ref.15. Source: EcoCyc cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	L-cysteine desulfhydrase activity Inferred from mutant phenotype PubMed 12883870. Source: EcoCyc identical protein binding Inferred from direct assay PubMed 4551942. Source: EcoCyc potassium ion binding Inferred from direct assay Ref.16. Source: EcoCyc pyridoxal phosphate binding Inferred from direct assay PubMed 4573978. Source: EcoCyc tryptophanase activity Inferred from direct assay PubMed 14017164PubMed 4573978. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	1	EBI-371316,EBI-542092
tauA	Q47537	1	EBI-371316,EBI-1116148

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 471

471

Tryptophanase HAMAP-Rule MF_00544

PRO_0000195611

Amino acid modifications

Modified residue

5

1

N6-acetyllysine Ref.14

Modified residue

115

1

N6-acetyllysine Ref.14

Modified residue

156

1

N6-acetyllysine Ref.14

Modified residue

270

1

N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_00544

Modified residue

450

1

N6-acetyllysine Ref.14

Experimental info

Mutagenesis

294

1

C → S: Identical to wild-type. Ref.11

Mutagenesis

298

1

C → S: Alters activity. Ref.11

Sequence conflict

137 – 140

4

DTTQ → TTQG no nucleotide entry Ref.1

Sequence conflict

379 – 380

2

QA → TG in AAA24676. Ref.1

Sequence conflict

379 – 380

2

QA → TG in CAA34096. Ref.2

Secondary structure

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471

Helix Strand Turn

Details...

Beta strand

10 – 18

9

Helix

24 – 33

10

Turn

34 – 36

3

Helix

38 – 40

3

Helix

43 – 45

3

Beta strand

47 – 49

3

Helix

61 – 66

6

Helix

67 – 69

3

Beta strand

74 – 76

3

Helix

78 – 91

14

Beta strand

94 – 99

6

Turn

103 – 105

3

Helix

106 – 121

16

Turn

125 – 127

3

Beta strand

129 – 134

6

Helix

137 – 145

9

Beta strand

149 – 152

4

Turn

156 – 159

4

Turn

166 – 169

4

Helix

173 – 183

11

Helix

185 – 187

3

Beta strand

191 – 197

7

Helix

199 – 201

3

Helix

207 – 219

13

Beta strand

224 – 227

4

Helix

231 – 241

11

Helix

243 – 245

3

Helix

250 – 257

8

Helix

258 – 260

3

Beta strand

262 – 270

9

Beta strand

278 – 282

5

Helix

285 – 287

3

Helix

288 – 300

13

Turn

305 – 309

5

Helix

312 – 324

13

Helix

328 – 347

20

Beta strand

352 – 355

4

Beta strand

360 – 363

4

Helix

364 – 367

4

Helix

373 – 375

3

Helix

377 – 389

13

Beta strand

390 – 392

3

Beta strand

394 – 397

4

Helix

398 – 401

4

Turn

405 – 407

3

Beta strand

417 – 420

4

Turn

424 – 426

3

Helix

429 – 444

16

Helix

446 – 448

3

Beta strand

452 – 456

5

Beta strand

459 – 461

3

Helix

462 – 465

4

Beta strand

467 – 470

4

Sequences

	Sequence		Length	Mass (Da)
	P0A853 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 5AFC1F41BD9D0034	FASTA	471	52,773
	10 20 30 40 50 60 MENFKHLPEP FRIRVIEPVK RTTRAYREEA IIKSGMNPFL LDSEDVFIDL LTDSGTGAVT 70 80 90 100 110 120 QSMQAAMMRG DEAYSGSRSY YALAESVKNI FGYQYTIPTH QGRGAEQIYI PVLIKKREQE 130 140 150 160 170 180 KGLDRSKMVA FSNYFFDTTQ GHSQINGCTV RNVYIKEAFD TGVRYDFKGN FDLEGLERGI 190 200 210 220 230 240 EEVGPNNVPY IVATITSNSA GGQPVSLANL KAMYSIAKKY DIPVVMDSAR FAENAYFIKQ 250 260 270 280 290 300 REAEYKDWTI EQITRETYKY ADMLAMSAKK DAMVPMGGLL CMKDDSFFDV YTECRTLCVV 310 320 330 340 350 360 QEGFPTYGGL EGGAMERLAV GLYDGMNLDW LAYRIAQVQY LVDGLEEIGV VCQQAGGHAA 370 380 390 400 410 420 FVDAGKLLPH IPADQFPAQA LACELYKVAG IRAVEIGSFL LGRDPKTGKQ LPCPAELLRL 430 440 450 460 470 TIPRATYTQT HMDFIIEAFK HVKENAANIK GLTFTYEPKV LRHFTAKLKE V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the structural gene for tryptophanase of Escherichia coli K-12." Deeley M.C., Yanofsky C. J. Bacteriol. 147:787-796(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Role of cysteine residues in tryptophanase for monovalent cation-induced activation." Tokushige M., Tsujimoto N., Oda T., Honda T., Yumoto N., Ito S., Yamamoto M., Kim E.H., Hiragi Y. Biochimie 71:711-720(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IMPORTANCE OF CYS-298. Strain: B/1t7-A.
[3]	"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The chemical structure of tryptophanase from Escherichia coli. 3. Isolation and amino acid sequence of the tryptic peptides." Kagamiyama H., Matsubara H., Snell E.E. J. Biol. Chem. 247:1576-1586(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF TRYPTIC PEPTIDES. Strain: K12.
[7]	"Evidence for transcription antitermination control of tryptophanase operon expression in Escherichia coli K-12." Stewart V., Yanofsky C. J. Bacteriol. 164:731-740(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. Strain: K12.
[8]	"A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli." Sarsero J.P., Wookey P.J., Gollnick P.D., Yanofsky C., Pittard A.J. J. Bacteriol. 173:3231-3234(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 463-471.
[9]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[10]	"A role of RnlA in the RNase LS activity from Escherichia coli." Otsuka Y., Koga M., Iwamoto A., Yonesaki T. Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-8. Strain: K12.
[11]	"Evidence that cysteine 298 is in the active site of tryptophan indole-lyase." Phillips R.S., Gollnick P.D. J. Biol. Chem. 264:10627-10632(1989) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-294 AND CYS-298.
[12]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[13]	"Changes in Escherichia coli transcriptome during acclimatization at low temperature." Polissi A., De Laurentis W., Zangrossi S., Briani F., Longhi V., Pesole G., Deho G. Res. Microbiol. 154:573-580(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION. Strain: K12 / MG1655 / ATCC 47076.
[14]	"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 C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-115; LYS-156 AND LYS-450, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[15]	"Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli." Li G., Young K.D. Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. Strain: K12 / MG1655 / ATCC 47076.
[16]	"Structure of Escherichia coli tryptophanase." Ku S.Y., Yip P., Howell P.L. Acta Crystallogr. D 62:814-823(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH PYRIDOXAL PHOSPHATE, PYRIDOXAL PHOSPHATE AT LYS-270.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

WZEC. E65173.

RefSeq

NP_418164.4. NC_000913.2.
YP_491725.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P0A853.

SMR

P0A853. Positions 4-471.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31878N.

IntAct

P0A853. 11 interactions.

MINT

MINT-1267429.

STRING

511145.b3708.

PTM databases

PhosSite

P0810440.

2D gel databases

SWISS-2DPAGE

P0A853.

Proteomic databases

PaxDb

P0A853.

PRIDE

P0A853.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76731; AAC76731; b3708.
BAE77584; BAE77584; BAE77584.

GeneID

12933600.
948221.

KEGG

ecj:Y75_p3463.
eco:b3708.

PATRIC

32122911. VBIEscCol129921_3831.

Organism-specific databases

EchoBASE

EB0998.

EcoGene

EG11005. tnaA.

Phylogenomic databases

eggNOG

COG3033.

HOGENOM

HOG000057883.

KO

K01667.

OMA

GRGAENV.

ProtClustDB

PRK13238.

Enzyme and pathway databases

BioCyc

EcoCyc:TRYPTOPHAN-MONOMER.
ECOL316407:JW3686-MONOMER.
MetaCyc:TRYPTOPHAN-MONOMER.

UniPathway

UPA00332; UER00452.

Gene expression databases

Genevestigator

P0A853.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

HAMAP

MF_00544. Tryptophanase.

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.
[Graphical view]

Pfam

PF01212. Beta_elim_lyase. 1 hit.
[Graphical view]

PIRSF

PIRSF001386. Trpase. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR02617. tnaA_trp_ase. 1 hit.

PROSITE

PS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P0A853.

EvolutionaryTrace

P0A853.

Entry information

Entry name

TNAA_ECOLI

Accession

Primary (citable) accession number: P0A853
Secondary accession number(s): P00913, P78123, Q2M822

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program