ID   PALY_CAMSI              Reviewed;         714 AA.
AC   P45726;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL;
OS   Camellia sinensis (Tea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Theaceae; Camellia.
OX   NCBI_TaxID=4442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Yabukita; TISSUE=Leaf;
RX   AGRICOLA=IND20445290; DOI=10.1007/BF00223703;
RA   Matsumoto S., Takeuchi A., Hayatsu M., Kondo S.;
RT   "Molecular cloning of phenylalanine ammonia-lyase cDNA and classification
RT   of varieties and cultivars of tea plants (Camellia sinensis) using the tea
RT   PAL cDNA probe.";
RL   Theor. Appl. Genet. 89:671-675(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; D26596; BAA05643.1; -; mRNA.
DR   AlphaFoldDB; P45726; -.
DR   SMR; P45726; -.
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..714
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215387"
FT   ACT_SITE        106
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         382
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         485
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         201
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        200..202
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   714 AA;  77752 MW;  5F0EC7E8D0AB9071 CRC64;
     MDSTTAIGNG VGSGGSPGFC LKDPLNWGVA AEAMKGSHLE EVKGMVEEFR KPVVRLGGET
     LTISQVAAIA VRGSEVAVEL SESAREGVKA SSDWVMESMN KGTDSYGVTT GFGATSHRRT
     KEGGALQKEL IRFLNAGIFG NGTESCHTLP QSATRAAMLV RINTLLQGYS GIRFEILEAI
     SKFLNNNITP CLPLRGTITA SGDLVPLSYI AGLLTGRHNS KAVGPTGEIL HPKEAFRLAG
     VEGGFFELQP KEGLALVNGT AVGSGLASMV LFEANILAVL SEVLSAIFAE VMQGKPEFTD
     HLTHKLKHHP GQIEAAAIME HILDGSSYVK AAQKLHEMDP LQKPKQDRYA LRTSPQWLGP
     LIEVIRSSTK SIEREINSVN DNPLINVSRN KALHGGNFQG TPIGVSMDNT RLAVASIGKL
     MFAQFSELVN DFYNNGLPSN LSGGRNPSLD YGFKGAEIAM AAYCSELQFL ANPVTNHVQS
     AEQHNQDVNS LGLISSRKTA EAVDILKLMS STYLVALCQA VDLRHFEENL RNTVKSTVSQ
     VAKRVLTMGV NGELHPSRFC EKDLLRVVDR EYIFAYIDDP CSATYPLMQK LRQVLVEHAL
     KNGESEKNLS TSIFQKIRAF EEEIKTLLPK EVESTRAAIE NGNSAIPNRI KECRSYPLYK
     FVREELGTEL LTGEKVRSPG EEFDKVFTAL CKGEMIDPLM DCLKEWNGAP LPIC