ID   PAL1_SOLLC              Reviewed;         704 AA.
AC   P35511;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            Short=PAL;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Early PAK 7;
RA   Bloksberg L.N., Kado C.I.;
RL   Thesis (1991), University of California Davis, United States.
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   -!- RNA EDITING: Modified_positions=23;
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR   EMBL; M83314; AAA34179.2; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P35511; -.
DR   SMR; P35511; -.
DR   STRING; 4081.Solyc09g007920.2.1; -.
DR   PaxDb; P35511; -.
DR   PRIDE; P35511; -.
DR   InParanoid; P35511; -.
DR   BRENDA; 4.3.1.24; 3101.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P35511; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; TAS:AgBase.
DR   GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
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;
KW   Reference proteome; RNA editing.
FT   CHAIN           1..704
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215397"
FT   ACT_SITE        96
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         475
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         191
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        190..192
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   704 AA;  76877 MW;  B3ABC33A5C58D606 CRC64;
     MDLCKKSIND PLNWEMAADS LRGSHLDEVK KMVDEFRKPI VKLGGETLSV AQVASIANVD
     DKSNGVKVEL SESARAGVKA SSDWVMDSMS KGTDSYGVTA GFGATSHRRT KNGGALQKEL
     IRFLNAGVFG NGIESFHTLP HSATRAAMLV RINTLLQGYS GIRFEILEAI TKLINSNITP
     CLPLRGTITA SGDLVPLSYI AGLLTGRPNS KAVGPNGEKL NAEEAFCVAG ISGGFFELQP
     KEGLALVNGT AVGSAMASIV LFESNIFAVM SEVLSAIFTE VMNGKPEFTD YLTHKLKHHP
     GQIEAAAIME HILDGSSYVK VAQKLHEMDP LQKPKQDRYA LRTSPQWLGP QIEVIRAATK
     MIEREINSVN DNPLIDVSRN KALHGGNFQG TPIGVSMDNT RLALASIGKL MFAQFSELVN
     DYYNNGLPSN LTAGRNPSLD YGFKGAEIAM ASYCSELQFL ANPVTNHVQS AEQHNQDVNS
     LGLISARKTA KAVDILKIMS STYLVALCQA IDLRHLEENL KSVVKNTVSQ VAKRTLTMGA
     NGELHPARFS EKELLRVVDR EYLFAYADDP CSSNYPLMQK LRQVLVDQAM KNGESEKNVN
     SSIFQKIGAF EDELIAVLPK EVESVRAVFE SGNPLIRNRI TECRSYPLYR LVREELGTEL
     LTGEKVRSPG EEIDKVFTAI CNGQIIDPLL ECLKSWNGAP LPIC