Tryptophanase - Escherichia coli O157:H7

Contribute

Send feedback

Read comments (?) or add your own

Q8XB34 (TNAA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	Z5203, ECs4645

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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 MF_00544
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_00544
Pathway	Amino-acid degradation; L-tryptophan degradation via pyruvate pathway; indole and pyruvate from L-tryptophan: step 1/1. HAMAP MF_00544
Subunit structure	Homotetramer By similarity. HAMAP MF_00544
Sequence similarities	Belongs to the beta-eliminating lyase family.
Sequence caution	The sequence AAG58908.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB38068.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 471

471

Tryptophanase HAMAP MF_00544

PRO_0000195612

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

115

N6-acetyllysine By similarity

Modified residue

156

N6-acetyllysine By similarity

Modified residue

270

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

450

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8XB34 [UniParc].

Last modified March 27, 2002. Version 1.
Checksum: 49DD2D41BD9D0034
Show »

FASTA

471

52,789

        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 HVKENASNIK GLTFTYEPKV LRHFTAKLKE V

« Hide

References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG58908.1. Different initiation. BA000007 Genomic DNA. Translation: BAB38068.1. Different initiation.
PIR	E91209. H86055.
RefSeq	NP_290344.1. NC_002655.2. NP_312672.2. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8XB34.
SMR	Q8XB34. Positions 4-471.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025459; EBESCP00000024352; EBESCG00000024512. EBESCT00000056410; EBESCP00000054238; EBESCG00000055458.
GeneID	915393. 960743.
GenomeReviews	Gene locus Z5203 in contig AE005174_GR. Gene locus ECs4645 in contig BA000007_GR.
KEGG	ece:Z5203. ecs:ECs4645.
PATRIC	18358895. VBIEscCol44059_4612.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000011364.
HOGENOM	HBG297784.
OMA	IYFSARK.
ProtClustDB	PRK13238.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS4645-MONOMER.
Family and domain databases
HAMAP	MF_00544. Tryptophanase. [Tree]
InterPro	IPR001597. ArAA_b-elim_lyase/Thr_aldolase. IPR011166. Beta-eliminating_lyase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. IPR013440. TNase. IPR018176. Tryptophanase_CS. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K01667.
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...

Entry information

Entry name

TNAA_ECO57

Accession

Primary (citable) accession number: Q8XB34

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	March 27, 2002
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents