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P31013 (TPL_CITFR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine phenol-lyase

EC=4.1.99.2
Alternative name(s):
Beta-tyrosinase
Gene names
Name:tpl
OrganismCitrobacter freundii
Taxonomic identifier546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-tyrosine + H2O = phenol + pyruvate + NH3. HAMAP-Rule MF_00543

Cofactor

Pyridoxal phosphate.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the beta-eliminating lyase family.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtyrosine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionpyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

tyrosine phenol-lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Tyrosine phenol-lyase HAMAP-Rule MF_00543
PRO_0000195631

Amino acid modifications

Modified residue2571N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_00543

Experimental info

Sequence conflict2051E → A in AAA23098. Ref.2

Secondary structure

........................................................................................ 456
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31013 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: B77AB58233C22474

FASTA45651,500
        10         20         30         40         50         60 
MNYPAEPFRI KSVETVSMIP RDERLKKMQE AGYNTFLLNS KDIYIDLLTD SGTNAMSDKQ 

        70         80         90        100        110        120 
WAGMMMGDEA YAGSENFYHL ERTVQELFGF KHIVPTHQGR GAENLLSQLA IKPGQYVAGN 

       130        140        150        160        170        180 
MYFTTTRYHQ EKNGAVFVDI VRDEAHDAGL NIAFKGDIDL KKLQKLIDEK GAENIAYICL 

       190        200        210        220        230        240 
AVTVNLAGGQ PVSMANMRAV RELTEAHGIK VFYDATRCVE NAYFIKEQEQ GFENKSIAEI 

       250        260        270        280        290        300 
VHEMFSYADG CTMSGKKDCL VNIGGFLCMN DDEMFSSAKE LVVVYEGMPS YGGLAGRDME 

       310        320        330        340        350        360 
AMAIGLREAM QYEYIEHRVK QVRYLGDKLK AAGVPIVEPV GGHAVFLDAR RFCEHLTQDE 

       370        380        390        400        410        420 
FPAQSLAASI YVETGVRSME RGIISAGRNN VTGEHHRPKL ETVRLTIPRR VYTYAHMDVV 

       430        440        450 
ADGIIKLYQH KEDIRGLKFI YEPKQLRFFT ARFDYI 

« Hide

References

[1]"Structure of tyrosine phenol-lyase genes from Citrobacter freundii and structural comparison with tryptophanase from Escherichia coli."
Iwamori S., Yoshino S., Ishiwata K., Makiguchi N.
J. Ferment. Bioeng. 72:147-151(1991)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 8090 / DSM 30039 / JCM 1657 / LMG 3246 / NCTC 9750.
[2]"Three-dimensional structure of tyrosine phenol-lyase."
Antson A.A., Demidkina T.V., Gollnick P., Dauter Z., Vontersch R., Long J., Berezhnoy S.N., Phillips R.S., Harutyunyan D., Wilson K.S.
Biochemistry 32:4195-4206(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 254-269; 275-299 AND 303-310, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-257.
[3]"The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzyme."
Antson A.A., Strokopytov B.V., Murshudov G.N., Isupov M.N., Harutyunyan E.H., Demidkina T.V., Vassylyev D.G., Dauter Z., Terry H., Wilson K.S.
FEBS Lett. 302:256-260(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[4]"The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity."
Sundararaju B., Antson A.A., Phillips R.S., Demidkina T.V., Barbolina M.V., Gollnick P., Dodson G.G., Wilson K.S.
Biochemistry 36:6502-6510(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66978 Genomic DNA. Translation: CAA47388.1.
L10821 Genomic DNA. Translation: AAA23098.1.
PIRA49493.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TPLX-ray2.30A/B1-456[»]
2EZ1X-ray1.90A/B1-456[»]
2EZ2X-ray1.85A/B1-456[»]
2TPLX-ray2.50A/B1-456[»]
2VLFX-ray1.89A/B1-456[»]
2VLHX-ray1.95A/B1-456[»]
2YCNX-ray2.04A/B1-456[»]
2YCPX-ray2.00A/B/C/D1-456[»]
2YCTX-ray2.25A/B1-456[»]
2YHKX-ray1.91A/B1-456[»]
ProteinModelPortalP31013.
SMRP31013. Positions 1-456.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00543. Tyr_phenol_lyase.
InterProIPR001597. 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.
IPR018176. Tryptophanase_CS.
IPR013441. Tyr_phenol_ly.
[Graphical view]
PfamPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFPIRSF001386. Trpase. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR02618. tyr_phenol_ly. 1 hit.
PROSITEPS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP31013.

Entry information

Entry nameTPL_CITFR
AccessionPrimary (citable) accession number: P31013
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references