ID   PALY_VITVI              Reviewed;         416 AA.
AC   P45735;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
DE   Flags: Fragment;
GN   Name=PAL;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8193299; DOI=10.1007/bf00029856;
RA   Sparvoli F., Martin C., Scienza A., Gavazzi G., Tonelli C.;
RT   "Cloning and molecular analysis of structural genes involved in flavonoid
RT   and stilbene biosynthesis in grape (Vitis vinifera L.).";
RL   Plant Mol. Biol. 24:743-755(1994).
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; X75967; CAA53581.1; -; mRNA.
DR   AlphaFoldDB; P45735; -.
DR   SMR; P45735; -.
DR   STRING; 29760.VIT_16s0039g01170.t01; -.
DR   PRIDE; P45735; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   BRENDA; 4.3.1.24; 6671.
DR   UniPathway; UPA00713; UER00725.
DR   ExpressionAtlas; P45735; baseline and differential.
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   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR008948; L-Aspartase-like.
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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT   CHAIN           <1..416
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215427"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   NON_TER         1
SQ   SEQUENCE   416 AA;  46015 MW;  F0E100FB35F0EFAE CRC64;
     TDHLTHKLKH HPGQIEAAAI MEHILDGSSY VKEAKKLHEM DPLQKPKQDR YALRTSPQWL
     GPHIEVIRAS TKSIEREINS VNDNPLIDVS RNKALHGGNF QGTPIGVSMD NTRLAIAAIG
     KLMFAQFSEL VNDFYNNGLP SNLSGSRNPS LDYGFKGAEI AMASYCSELQ FLANPVTNHV
     ESAEQHNQDV NSLGLISSRK TAEAVDILKL MSTTYLVALC QAIDLRHLEE NLKSTVKKTV
     SHVAKKTLTI GANGELHPSR FCEKDLLKVV DREHVFAYID DPCSATYPLM QKVRQVLVEH
     ALNNGESEKN GSTSIFQKIG AFEEELKAVL PKEVESARDG VESGNPSIPN RIKECRSYPL
     YKFVREELGT GLLTGEKVRS PGEDFDKVFT AMCEGKIIDP LLDCLSAWNG APLPIC