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Protein

Phenylalanine/tyrosine ammonia-lyase

Gene

PAL

Organism
Rhodosporidium toruloides (Yeast) (Rhodotorula gracilis)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the non-oxidative deamination of L-phenylalanine and L-tyrosine to form trans-cinnamic acid and p-coumaric acid respectively with similar efficiencies. Facilitates the commitment step in phenylpropanoid pathways that produce lignins, coumarins and flavonoids.1 Publication

Catalytic activityi

L-phenylalanine = trans-cinnamate + ammonia.1 Publication
L-tyrosine = trans-p-hydroxycinnamate + ammonia.1 Publication

Kineticsi

  1. KM=0.29 mM for L-phenylalanine2 Publications
  2. KM=0.18 mM for L-tyrosine2 Publications

    pH dependencei

    Optimum pH is 8.5.2 Publications

    Pathwayi: trans-cinnamate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes trans-cinnamate from L-phenylalanine.
    Proteins known to be involved in this subpathway in this organism are:
    1. Phenylalanine/tyrosine ammonia-lyase (PAL), Phenylalanine ammonia-lyase (RHTO0S_04e04676g), Phenylalanine ammonia-lyase (FGENESH: predicted gene_9.166), Phenylalanine ammonia-lyase (AAT19DRAFT_16462)
    This subpathway is part of the pathway trans-cinnamate biosynthesis, which is itself part of Phenylpropanoid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes trans-cinnamate from L-phenylalanine, the pathway trans-cinnamate biosynthesis and in Phenylpropanoid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei110Proton donor/acceptorBy similarity1
    Binding sitei366SubstrateBy similarity1
    Binding sitei468Substrate1 Publication1
    Binding sitei496Substrate1 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionLyase
    Biological processPhenylpropanoid metabolism

    Enzyme and pathway databases

    BRENDAi4.3.1.24 5424
    UniPathwayi
    UPA00713;UER00725

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine/tyrosine ammonia-lyase (EC:4.3.1.25)
    Alternative name(s):
    Bifunctional phenylalanine ammonia-lyase
    Short name:
    Bifunctional PAL
    Gene namesi
    Name:PAL
    OrganismiRhodosporidium toruloides (Yeast) (Rhodotorula gracilis)
    Taxonomic identifieri5286 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaPucciniomycotinaMicrobotryomycetesSporidiobolalesSporidiobolaceaeRhodotorula

    Subcellular locationi

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002154321 – 716Phenylalanine/tyrosine ammonia-lyaseAdd BLAST716

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Cross-linki211 ↔ 2135-imidazolinone (Ala-Gly)1 Publication
    Modified residuei2122,3-didehydroalanine (Ser)1 Publication1

    Post-translational modificationi

    Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.

    Proteomic databases

    PRIDEiP11544

    Interactioni

    Subunit structurei

    Homotetramer. Dimer of dimers.2 Publications

    Structurei

    Secondary structure

    1716
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP11544
    SMRiP11544
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11544

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PAL/histidase family.Curated

    Family and domain databases

    CDDicd00332 PAL-HAL, 1 hit
    Gene3Di1.10.274.20, 1 hit
    1.10.275.10, 1 hit
    InterProiView protein in InterPro
    IPR001106 Aromatic_Lyase
    IPR024083 Fumarase/histidase_N
    IPR008948 L-Aspartase-like
    IPR022313 Phe/His_NH3-lyase_AS
    IPR005922 Phe_NH3-lyase
    IPR023144 Phe_NH3-lyase_shielding_dom_sf
    PANTHERiPTHR10362 PTHR10362, 1 hit
    PfamiView protein in Pfam
    PF00221 Lyase_aromatic, 1 hit
    SUPFAMiSSF48557 SSF48557, 1 hit
    TIGRFAMsiTIGR01226 phe_am_lyase, 1 hit
    PROSITEiView protein in PROSITE
    PS00488 PAL_HISTIDASE, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P11544-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAPSLDSISH SFANGVASAK QAVNGASTNL AVAGSHLPTT QVTQVDIVEK
    60 70 80 90 100
    MLAAPTDSTL ELDGYSLNLG DVVSAARKGR PVRVKDSDEI RSKIDKSVEF
    110 120 130 140 150
    LRSQLSMSVY GVTTGFGGSA DTRTEDAISL QKALLEHQLC GVLPSSFDSF
    160 170 180 190 200
    RLGRGLENSL PLEVVRGAMT IRVNSLTRGH SAVRLVVLEA LTNFLNHGIT
    210 220 230 240 250
    PIVPLRGTIS ASGDLSPLSY IAAAISGHPD SKVHVVHEGK EKILYAREAM
    260 270 280 290 300
    ALFNLEPVVL GPKEGLGLVN GTAVSASMAT LALHDAHMLS LLSQSLTAMT
    310 320 330 340 350
    VEAMVGHAGS FHPFLHDVTR PHPTQIEVAG NIRKLLEGSR FAVHHEEEVK
    360 370 380 390 400
    VKDDEGILRQ DRYPLRTSPQ WLGPLVSDLI HAHAVLTIEA GQSTTDNPLI
    410 420 430 440 450
    DVENKTSHHG GNFQAAAVAN TMEKTRLGLA QIGKLNFTQL TEMLNAGMNR
    460 470 480 490 500
    GLPSCLAAED PSLSYHCKGL DIAAAAYTSE LGHLANPVTT HVQPAEMANQ
    510 520 530 540 550
    AVNSLALISA RRTTESNDVL SLLLATHLYC VLQAIDLRAI EFEFKKQFGP
    560 570 580 590 600
    AIVSLIDQHF GSAMTGSNLR DELVEKVNKT LAKRLEQTNS YDLVPRWHDA
    610 620 630 640 650
    FSFAAGTVVE VLSSTSLSLA AVNAWKVAAA ESAISLTRQV RETFWSAAST
    660 670 680 690 700
    SSPALSYLSP RTQILYAFVR EELGVKARRG DVFLGKQEVT IGSNVSKIYE
    710
    AIKSGRINNV LLKMLA
    Length:716
    Mass (Da):76,880
    Last modified:November 1, 1990 - v2
    Checksum:i0C1DF61769A4E5E6
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti4 – 37SLDSI…AGSHL → RPTSQSQARTC in AAA33883 (PubMed:2828184).CuratedAdd BLAST34

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X51513 Genomic DNA Translation: CAA35886.1
    M18261 Genomic DNA Translation: AAA33883.1
    X12702 mRNA Translation: CAA31209.1
    PIRiA29607
    A56628

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X51513 Genomic DNA Translation: CAA35886.1
    M18261 Genomic DNA Translation: AAA33883.1
    X12702 mRNA Translation: CAA31209.1
    PIRiA29607
    A56628

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1T6JX-ray2.10A/B1-716[»]
    1T6PX-ray2.70A/B/C/D/E/F/G/H1-716[»]
    1Y2MX-ray1.60A/B/C/D1-716[»]
    ProteinModelPortaliP11544
    SMRiP11544
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiP11544

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayi
    UPA00713;UER00725

    BRENDAi4.3.1.24 5424

    Miscellaneous databases

    EvolutionaryTraceiP11544

    Family and domain databases

    CDDicd00332 PAL-HAL, 1 hit
    Gene3Di1.10.274.20, 1 hit
    1.10.275.10, 1 hit
    InterProiView protein in InterPro
    IPR001106 Aromatic_Lyase
    IPR024083 Fumarase/histidase_N
    IPR008948 L-Aspartase-like
    IPR022313 Phe/His_NH3-lyase_AS
    IPR005922 Phe_NH3-lyase
    IPR023144 Phe_NH3-lyase_shielding_dom_sf
    PANTHERiPTHR10362 PTHR10362, 1 hit
    PfamiView protein in Pfam
    PF00221 Lyase_aromatic, 1 hit
    SUPFAMiSSF48557 SSF48557, 1 hit
    TIGRFAMsiTIGR01226 phe_am_lyase, 1 hit
    PROSITEiView protein in PROSITE
    PS00488 PAL_HISTIDASE, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPALY_RHOTO
    AccessioniPrimary (citable) accession number: P11544
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 1, 1990
    Last modified: January 31, 2018
    This is version 114 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure
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    Main funding by: National Institutes of Health

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