ID   PAL1_PRUAV              Reviewed;         717 AA.
AC   O64963;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Phenylalanine ammonia-lyase 1;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL1;
OS   Prunus avium (Cherry) (Cerasus avium).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=42229;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Summit;
RA   Wiersma P.A., Wu Z.;
RT   "A full-length cDNA for phenylalanine ammonia-lyase cloned from ripe Sweet
RT   Cherry fruit (Prunus avium).";
RL   (er) Plant Gene Register PGR98-184(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; AF036948; AAC78457.1; -; mRNA.
DR   AlphaFoldDB; O64963; -.
DR   SMR; O64963; -.
DR   PRIDE; O64963; -.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000515124; Unplaced.
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;
KW   Reference proteome.
FT   CHAIN           1..717
FT                   /note="Phenylalanine ammonia-lyase 1"
FT                   /id="PRO_0000215417"
FT   ACT_SITE        109
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         488
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         204
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        203..205
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   717 AA;  78000 MW;  B84DF90FA0BF60B3 CRC64;
     MATNSIKQNG HKNGSVELPE LCIKKDPLNW GVAAETLKGS HLDEVKRMVA EYRKPVVKLG
     GESLTISQVA AIATHDSGVK VELSESARAG VKASSDWVMD SMSKGTDSYG VTTGFGATSH
     RRTKQGAALQ KELIRFLNAG VFGSTKESGH TLPHQATRAA MLVRINTLLQ GYSGIRFEIL
     EVITKFLNNN VTPCLPLRGT ITASGDLVPL SYIAGMLTGR PNSKAVGPDG QTLSAAEAFE
     FVGINSGFFE LQPKEGLALV NGTAVGSGLA STVLFDTNIL ALLSEILSAI FAEVMQGKPE
     FTDHLTHKLK HHPGQIEAAA IMEHILDGSS YVKAAKKLHE QDPLQKPKQD RYALRTSPQW
     LGPQIEVIRY STKSIEREID SVNDNPLIDV SRNKALHGGN FQGTPIGVSM DNTRLAIASI
     GKLMFAQFSE LVNDFYNNGL PSNLSGGRNP SLDYGFKGAE IAMASYCSEL QFLANPVTNH
     VQSAEQHNQD VNSLGLISSR KTAEAVDILK LMSSTFLVAL CQAIDLRHLE ENLRNTVKNT
     VSQVAKRTLT TGVNGELHPS RFCEKDLLKV VDREYVFAYI DDPCSATYPL MQKLRQVLVE
     HALTNGENEK NASTSIFQKI VAFEEELKVL LPKEVDSARA ALDSGSAGVP NRITECRSYP
     LYKFVREELG AEYLTGEKVR SPGEECDKVF TAICEGKIID PILDCLEGWN GAPLPIC