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P31013

- TPL_CITFR

UniProt

P31013 - TPL_CITFR

Protein

Tyrosine phenol-lyase

Gene

tpl

Organism
Citrobacter freundii
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.

    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

    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 – 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.
    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

    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

    Experimental Info

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

    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...
    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: October 1, 2014
    This is version 93 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