ID   PAL5_SOLLC              Reviewed;         721 AA.
AC   P26600;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            Short=PAL;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL5;
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. Bonny Best;
RX   PubMed=1601854; DOI=10.1016/s0021-9258(19)49773-1;
RA   Lee S.-W., Robb E.J., Nazar R.N.;
RT   "Truncated phenylalanine ammonia-lyase expression in tomato (Lycopersicon
RT   esculentum).";
RL   J. Biol. Chem. 267:11824-11830(1992).
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; M90692; AAA34176.1; -; Genomic_DNA.
DR   PIR; A44133; A44133.
DR   AlphaFoldDB; P26600; -.
DR   SMR; P26600; -.
DR   STRING; 4081.Solyc09g007910.2.1; -.
DR   PaxDb; P26600; -.
DR   PRIDE; P26600; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   InParanoid; P26600; -.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P26600; 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   3: Inferred from homology;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism;
KW   Reference proteome.
FT   CHAIN           1..721
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215398"
FT   ACT_SITE        113
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         389
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         492
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         208
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        207..209
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   721 AA;  78496 MW;  31B4772693D150E7 CRC64;
     MASSIVQNGH VNGEAMDLCK KSINVNDPLN WEMAAESLRG SHLDEVKKMV DEFRKPIVKL
     GGETLTVAQV ASIANVDNKS NGVKVELSES ARAGVKASSD WVMDSMGKGT DSYGVTTGFG
     ATSHRRTKNG GALQKELIRF LNAGVFGNGT ESSHTLPHSA TRAAMLVRIN TLLQGYSGIR
     FEILEAITKL INSNITPCLP LRGTITASGD LVPLSYIAGL LTGRPNSKAV GPNGEKLNAE
     ERFRVAGVTS GFFELQPKEG LALVNGTAVG SGMASMVLFE SNILAVMSEV LSAIFAEVMN
     GKPEFTDYLT HKLKHHPGQI EAAAIMEHIL DGSSYVKAAQ KLHEMDPLQK PKQDRYALRT
     SPQWLGPQIE VIRAATKMIE REINSVNDNP LIDVSRNKAL HGGNFQGTPI GVSMDNTRLA
     LASIGKLMFA QFSELVNDYY NNGLPLNLTA GRNPSLDYGL KGAEIAMASY CSELQFLANP
     VTNHVQSAEQ HNQDVNSLGL ISARKTAEAV DILKLMSSTY LVALCQAIDL RHLEENLKNA
     VKNTVSQVAK KTLAMGANGE LHPARFCEKE LLQVVEREYL FTYADDPCSS TYPLMQKLRQ
     VLVDHAMKNG ESEKNLNSSI FQKIVAFEDE LKAVLPKEVE SARAVVESGN PAIPNRITEC
     RSYPLYRLVR QEVGTELLTG EKVRSPGEEI DKVFTAFCNG QIIDPLLECL KSWNGAPIPI
     C