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Protein

Tyrosine phenol-lyase

Gene

tpl

Organism
Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-tyrosine + H2O = phenol + pyruvate + NH3.

Cofactori

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine phenol-lyase (EC:4.1.99.2)
Alternative name(s):
Beta-tyrosinase
Gene namesi
Name:tpl
Synonyms:tutA
OrganismiEnterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Taxonomic identifieri549 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePantoeaPantoea agglomerans group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Tyrosine phenol-lyasePRO_0000195633Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

Contains L-DOPA (3',4'-dihydroxyphenylalanine).

Expressioni

Inductioni

By L-tyrosine.

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159Combined sources
Helixi21 – 3010Combined sources
Turni31 – 333Combined sources
Helixi35 – 373Combined sources
Helixi40 – 423Combined sources
Beta strandi44 – 463Combined sources
Beta strandi50 – 523Combined sources
Helixi58 – 636Combined sources
Beta strandi71 – 733Combined sources
Helixi75 – 8814Combined sources
Beta strandi91 – 988Combined sources
Helixi99 – 11012Combined sources
Beta strandi115 – 1217Combined sources
Helixi124 – 1329Combined sources
Beta strandi135 – 1395Combined sources
Helixi143 – 1464Combined sources
Helixi160 – 17011Combined sources
Helixi172 – 1743Combined sources
Beta strandi175 – 18410Combined sources
Turni185 – 1884Combined sources
Helixi194 – 20714Combined sources
Beta strandi211 – 2144Combined sources
Helixi218 – 22811Combined sources
Helixi237 – 2459Combined sources
Beta strandi249 – 2546Combined sources
Turni255 – 2595Combined sources
Beta strandi265 – 2706Combined sources
Helixi272 – 28514Combined sources
Turni289 – 2935Combined sources
Helixi296 – 30914Combined sources
Helixi312 – 33120Combined sources
Beta strandi342 – 3487Combined sources
Helixi349 – 3524Combined sources
Helixi358 – 3603Combined sources
Helixi362 – 37413Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi379 – 3824Combined sources
Helixi383 – 3864Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi402 – 4065Combined sources
Helixi414 – 42815Combined sources
Helixi429 – 4335Combined sources
Beta strandi437 – 4415Combined sources
Beta strandi444 – 4463Combined sources
Helixi447 – 4504Combined sources
Beta strandi452 – 4554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7GX-ray2.10A/B/C/D1-456[»]
ProteinModelPortaliP31011.
SMRiP31011. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31011.

Family & Domainsi

Sequence similaritiesi

Belongs to the beta-eliminating lyase family.Curated

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00543. Tyr_phenol_lyase.
InterProiIPR001597. 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]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF001386. Trpase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02618. tyr_phenol_ly. 1 hit.
PROSITEiPS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31011-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYPAEPFRI KSVETVSMIS RDERVKKMQE AGYNTFLLNS KDIYIDLLTD
60 70 80 90 100
SGTNAMSDKQ WAGMMIGDEA YAGSENFYHL EKTVKELFGF KHIVPTHQGR
110 120 130 140 150
GAENLLSQLA IKPGQYVAGN MYFTTTRFHQ EKNGATFVDI VRDEAHDASL
160 170 180 190 200
NLPFKGDIDL NKLATLIKEK GAENIAYICL AVTVNLAGGQ PVSMANMRAV
210 220 230 240 250
HEMASTYGIK IFYDATRCVE NAYFIKEQEA GYENVSIKDI VHEMFSYADG
260 270 280 290 300
CTMSGKKDCL VNIGGFLCMN DEEMFSAAKE LVVVYEGMPS YGGLAGRDME
310 320 330 340 350
AMAIGLREAM QYEYIEHRVK QVRYLGDKLR EAGVPIVEPT GGHAVFLDAR
360 370 380 390 400
RFCPHLTQDQ FPAQSLAASI YMETGVRSME RGIVSAGRSK ETGENHRPKL
410 420 430 440 450
ETVRLTIPRR VYTYAHMDVV ADGIIKLYQH KEDIRGLTFV YEPKQLRFFT

ARFDFI
Length:456
Mass (Da):51,365
Last modified:February 1, 1996 - v2
Checksum:i34758B48AF7C4AE2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 1571D → N in strain: MT-10509.
Natural varianti212 – 2121F → Y in strain: MT-10509.
Natural varianti397 – 3971R → S in strain: MT-10509.
Natural varianti420 – 4201V → I in strain: MT-10509.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50513 Genomic DNA. Translation: AAB24234.1.
D13714 Genomic DNA. Translation: BAA02867.1.
U25347 Genomic DNA. Translation: AAA66390.1.
L08484 Genomic DNA. Translation: AAA71928.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50513 Genomic DNA. Translation: AAB24234.1.
D13714 Genomic DNA. Translation: BAA02867.1.
U25347 Genomic DNA. Translation: AAA66390.1.
L08484 Genomic DNA. Translation: AAA71928.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7GX-ray2.10A/B/C/D1-456[»]
ProteinModelPortaliP31011.
SMRiP31011. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP31011.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00543. Tyr_phenol_lyase.
InterProiIPR001597. 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]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF001386. Trpase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR02618. tyr_phenol_ly. 1 hit.
PROSITEiPS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of the Erwinia herbicola tyrosine phenol-lyase gene in Escherichia coli."
    Iwamori S., Oikawa T., Ishiwata K., Makiguchi N.
    Biotechnol. Appl. Biochem. 16:77-85(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MT-10509.
  2. "Cloning and nucleotide sequence of Erwinia herbicola AJ2982 tyrosine phenol-lyase gene."
    Suzuki H., Nishihara K., Usui N., Matsui H., Kumagai H.
    J. Ferment. Bioeng. 75:145-148(1993)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11.
    Strain: AJ2982.
  3. Foor F.
    Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 21434 / AJ 2985.
  4. "Production of L-dihydroxyphenylalanine in Escherichia coli with the tyrosine phenol-lyase gene cloned from Erwinia herbicola."
    Foor F., Morin N., Bostian K.
    Appl. Environ. Microbiol. 59:3070-3075(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.

Entry informationi

Entry nameiTPL_ENTAG
AccessioniPrimary (citable) accession number: P31011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: October 14, 2015
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.