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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.

Cofactori

GO - Molecular functioni

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

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-lyasePRO_0000195631Add
BLAST

Amino acid modifications

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

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 – 647Combined sources
Beta strandi71 – 733Combined sources
Helixi75 – 8814Combined sources
Beta strandi91 – 988Combined sources
Helixi99 – 11012Combined sources
Beta strandi116 – 1216Combined sources
Helixi124 – 1329Combined sources
Beta strandi136 – 1394Combined sources
Helixi143 – 1464Combined sources
Turni153 – 1564Combined sources
Helixi160 – 17011Combined sources
Helixi172 – 1743Combined sources
Beta strandi175 – 18410Combined sources
Turni185 – 1884Combined sources
Helixi194 – 20613Combined 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
Turni353 – 3553Combined sources
Helixi358 – 3603Combined sources
Helixi362 – 37413Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi379 – 3824Combined sources
Helixi383 – 3864Combined sources
Turni390 – 3923Combined sources
Beta strandi402 – 4065Combined sources
Turni409 – 4113Combined sources
Helixi414 – 42916Combined sources
Helixi430 – 4334Combined sources
Beta strandi437 – 4415Combined sources
Beta strandi444 – 4463Combined sources
Helixi447 – 4493Combined sources
Beta strandi452 – 4554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31013.

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.

P31013-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNYPAEPFRI KSVETVSMIP RDERLKKMQE AGYNTFLLNS KDIYIDLLTD
60 70 80 90 100
SGTNAMSDKQ WAGMMMGDEA YAGSENFYHL ERTVQELFGF KHIVPTHQGR
110 120 130 140 150
GAENLLSQLA IKPGQYVAGN MYFTTTRYHQ EKNGAVFVDI VRDEAHDAGL
160 170 180 190 200
NIAFKGDIDL KKLQKLIDEK GAENIAYICL AVTVNLAGGQ PVSMANMRAV
210 220 230 240 250
RELTEAHGIK VFYDATRCVE NAYFIKEQEQ GFENKSIAEI VHEMFSYADG
260 270 280 290 300
CTMSGKKDCL VNIGGFLCMN DDEMFSSAKE LVVVYEGMPS YGGLAGRDME
310 320 330 340 350
AMAIGLREAM QYEYIEHRVK QVRYLGDKLK AAGVPIVEPV GGHAVFLDAR
360 370 380 390 400
RFCEHLTQDE FPAQSLAASI YVETGVRSME RGIISAGRNN VTGEHHRPKL
410 420 430 440 450
ETVRLTIPRR VYTYAHMDVV ADGIIKLYQH KEDIRGLKFI YEPKQLRFFT

ARFDYI
Length:456
Mass (Da):51,500
Last modified:July 1, 1993 - v1
Checksum:iB77AB58233C22474
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051E → A in AAA23098. (PubMed:7916622)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66978 Genomic DNA. Translation: CAA47388.1.
L10821 Genomic DNA. Translation: AAA23098.1.
PIRiA49493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66978 Genomic DNA. Translation: CAA47388.1 .
L10821 Genomic DNA. Translation: AAA23098.1 .
PIRi A49493.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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: November 26, 2014
This is version 94 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