B7NR10 (TNAA_ECO7I) 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
Ordered Locus Names:	ECIAI39_4312

Organism

Escherichia coli O7:K1 (strain IAI39 / ExPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585057 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-tryptophan + H2O = indole + pyruvate + NH3. HAMAP-Rule MF_00544
Cofactor	Pyridoxal phosphate By similarity. HAMAP-Rule MF_00544
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 By similarity. HAMAP-Rule MF_00544
Sequence similarities	Belongs to the beta-eliminating lyase family.

Ontologies

Keywords
Biological process	Tryptophan catabolism
Ligand	Pyridoxal phosphate
Molecular function	Lyase
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Molecular_function	pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro tryptophanase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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_1000128908
Amino acid modifications
	Modified residue	5	1	N6-acetyllysine By similarity
	Modified residue	115	1	N6-acetyllysine By similarity
	Modified residue	156	1	N6-acetyllysine By similarity
	Modified residue	270	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	450	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7NR10 [UniParc]. Last modified March 24, 2009. 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

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IAI39 / ExPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928164 Genomic DNA. Translation: CAR20418.1.
RefSeq	YP_002410187.1. NC_011750.1.
3D structure databases
ProteinModelPortal	B7NR10.
SMR	B7NR10. Positions 4-471.
ModBase	Search...
Protein-protein interaction databases
STRING	585057.ECIAI39_4312.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAR20418; CAR20418; ECIAI39_4312.
GeneID	7152995.
KEGG	ect:ECIAI39_4312.
PATRIC	18337569. VBIEscCol51957_4457.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3033.
HOGENOM	HOG000057883.
KO	K01667.
OMA	GRGAENV.
ProtClustDB	PRK13238.
Enzyme and pathway databases
BioCyc	ECOL585057:GJ8I-4462-MONOMER.
UniPathway	UPA00332; UER00452.
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	B7NR10.

Entry information

Entry name

TNAA_ECO7I

Accession

Primary (citable) accession number: B7NR10

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program