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P31013

- TPL_CITFR

UniProt

P31013 - TPL_CITFR

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Protein
Tyrosine phenol-lyase
Gene
tpl
Organism
Citrobacter freundii
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. tyrosine phenol-lyase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. tyrosine metabolic process Source: InterPro
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
OrganismiCitrobacter freundii
Taxonomic identifieri546 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Tyrosine phenol-lyaseUniRule annotation
PRO_0000195631Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159
Helixi21 – 3010
Turni31 – 333
Helixi35 – 373
Helixi40 – 423
Beta strandi44 – 463
Beta strandi50 – 523
Helixi58 – 647
Beta strandi71 – 733
Helixi75 – 8814
Beta strandi91 – 988
Helixi99 – 11012
Beta strandi116 – 1216
Helixi124 – 1329
Beta strandi136 – 1394
Helixi143 – 1464
Turni153 – 1564
Helixi160 – 17011
Helixi172 – 1743
Beta strandi175 – 18410
Turni185 – 1884
Helixi194 – 20613
Beta strandi211 – 2144
Helixi218 – 22811
Helixi237 – 2459
Beta strandi249 – 2546
Turni255 – 2595
Beta strandi265 – 2706
Helixi272 – 28514
Turni289 – 2935
Helixi296 – 30914
Helixi312 – 33120
Beta strandi342 – 3487
Helixi349 – 3524
Turni353 – 3553
Helixi358 – 3603
Helixi362 – 37413
Beta strandi375 – 3773
Beta strandi379 – 3824
Helixi383 – 3864
Turni390 – 3923
Beta strandi402 – 4065
Turni409 – 4113
Helixi414 – 42916
Helixi430 – 4334
Beta strandi437 – 4415
Beta strandi444 – 4463
Helixi447 – 4493
Beta strandi452 – 4554

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP31013.
SMRiP31013. Positions 1-456.

Miscellaneous databases

EvolutionaryTraceiP31013.

Family & Domainsi

Sequence similaritiesi

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.

P31013-1 [UniParc]FASTAAdd to Basket

« Hide

MNYPAEPFRI KSVETVSMIP RDERLKKMQE AGYNTFLLNS KDIYIDLLTD    50
SGTNAMSDKQ WAGMMMGDEA YAGSENFYHL ERTVQELFGF KHIVPTHQGR 100
GAENLLSQLA IKPGQYVAGN MYFTTTRYHQ EKNGAVFVDI VRDEAHDAGL 150
NIAFKGDIDL KKLQKLIDEK GAENIAYICL AVTVNLAGGQ PVSMANMRAV 200
RELTEAHGIK VFYDATRCVE NAYFIKEQEQ GFENKSIAEI VHEMFSYADG 250
CTMSGKKDCL VNIGGFLCMN DDEMFSSAKE LVVVYEGMPS YGGLAGRDME 300
AMAIGLREAM QYEYIEHRVK QVRYLGDKLK AAGVPIVEPV GGHAVFLDAR 350
RFCEHLTQDE FPAQSLAASI YVETGVRSME RGIISAGRNN VTGEHHRPKL 400
ETVRLTIPRR VYTYAHMDVV ADGIIKLYQH KEDIRGLKFI YEPKQLRFFT 450
ARFDYI 456
Length:456
Mass (Da):51,500
Last modified:July 1, 1993 - v1
Checksum:iB77AB58233C22474
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051E → A in AAA23098. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66978 Genomic DNA. Translation: CAA47388.1.
L10821 Genomic DNA. Translation: AAA23098.1.
PIRiA49493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66978 Genomic DNA. Translation: CAA47388.1 .
L10821 Genomic DNA. Translation: AAA23098.1 .
PIRi A49493.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TPL X-ray 2.30 A/B 1-456 [» ]
2EZ1 X-ray 1.90 A/B 1-456 [» ]
2EZ2 X-ray 1.85 A/B 1-456 [» ]
2TPL X-ray 2.50 A/B 1-456 [» ]
2VLF X-ray 1.89 A/B 1-456 [» ]
2VLH X-ray 1.95 A/B 1-456 [» ]
2YCN X-ray 2.04 A/B 1-456 [» ]
2YCP X-ray 2.00 A/B/C/D 1-456 [» ]
2YCT X-ray 2.25 A/B 1-456 [» ]
2YHK X-ray 1.91 A/B 1-456 [» ]
ProteinModelPortali P31013.
SMRi P31013. Positions 1-456.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P31013.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_00543. Tyr_phenol_lyase.
InterProi 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.
IPR018176. Tryptophanase_CS.
IPR013441. Tyr_phenol_ly.
[Graphical view ]
Pfami PF01212. Beta_elim_lyase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001386. Trpase. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR02618. tyr_phenol_ly. 1 hit.
PROSITEi PS00853. BETA_ELIM_LYASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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).

Entry informationi

Entry nameiTPL_CITFR
AccessioniPrimary (citable) accession number: P31013
Entry historyi
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 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

External Data

Dasty 3

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