ID   PALY_HELAN              Reviewed;         667 AA.
AC   O04058;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL;
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mazeyrat F.A., Salles S., Drevet J., Roeckel-Drevet P., Tourvieille D.,
RA   Ledoigt G.;
RT   "Isolation of a complete PAL cDNA from sunflower.";
RL   (er) Plant Gene Register PGR98-108(1998).
CC   -!- FUNCTION: This is a key enzyme of plant metabolism catalyzing the first
CC       reaction in the biosynthesis from L-phenylalanine of a wide variety of
CC       natural products based on the phenylpropane skeleton.
CC       {ECO:0000250|UniProtKB:P24481}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-phenylalanine = (E)-cinnamate + NH4(+);
CC         Xref=Rhea:RHEA:21384, ChEBI:CHEBI:15669, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58095; EC=4.3.1.24;
CC         Evidence={ECO:0000250|UniProtKB:P24481};
CC   -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC       trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P24481}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC       is formed autocatalytically by cyclization and dehydration of residues
CC       Ala-Ser-Gly. {ECO:0000250|UniProtKB:Q68G84}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR   EMBL; Y12461; CAA73065.1; -; mRNA.
DR   PIR; T12749; T12749.
DR   AlphaFoldDB; O04058; -.
DR   SMR; O04058; -.
DR   UniPathway; UPA00713; UER00725.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00332; PAL-HAL; 1.
DR   Gene3D; 1.10.274.20; -; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR   InterPro; IPR005922; Phe_NH3-lyase.
DR   InterPro; IPR023144; Phe_NH3-lyase_shielding_dom_sf.
DR   PANTHER; PTHR10362; PTHR10362; 1.
DR   Pfam; PF00221; Lyase_aromatic; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR01226; phe_am_lyase; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT   CHAIN           1..667
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215392"
FT   ACT_SITE        103
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         482
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         198
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        197..199
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   667 AA;  72076 MW;  FBD3DB590EE70AB2 CRC64;
     MENGTHVNGS ANGFCIKDPL NWGVAAEALT GSHLDEVKKM VGEFRKPVVK LGGETLTVSQ
     VAGISAAGDG NMVKVELSEA ARAGVKASSD WVMESMNKGT DSYGVTTGFG ATSHRRTKNG
     GALQKELIRF LNAGIFGNGT ESSHTLPHSA TRAAMLVRIN TLLQGYSGIR FEILEAITKF
     LNNNITPCLP LRGTITASGD LVPLSYIAGL LTGRPNSKAV GPAGEVLNAE SAFAQAGVEG
     GFFELQPKEG LALVNGTAVG SGMASMVLFE ANVLALLSEV LSAIFAEVMQ GKPEFTDHLT
     HKLKHHPGQI EAAAIMEYIL DGSDYVKAAQ KVHEMDPLQK PKQDRYALRT SPQWLGPQIE
     VIRSATKMIE REINSVNDNP LIDVSRNKAL HGGNFQGTPI GVSMDNTRLA IAAIGKVTIA
     QFSELVNDFY NNGLPSHLSG GRNPSLDSGF KGGEIAMASY CSELQFLANP VTNHVQSAEQ
     HNQDVNSLGL ISARKTAEAV DILKLMSSTY LVALCQSIDL RHLEENMKST VKNTVSQVAK
     KVLTMGVNGE LHPSRFCEKD LLRVVDREYV FAYADDPCLT TYPLMQKLRQ VLVDHALNNG
     ETEKNANTSI FQKIATFEDE LKAILPKEVE SVRVAFENGT MSIPNRIKAC RSYPLYRFVR
     EELGGAT