ID   PAL1_RUBID              Reviewed;         710 AA.
AC   Q9M568;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Phenylalanine ammonia-lyase 1;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
DE   AltName: Full=RiPAL1;
GN   Name=PAL1;
OS   Rubus idaeus (Raspberry).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC   Rubus.
OX   NCBI_TaxID=32247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fruit;
RX   PubMed=11553751; DOI=10.1104/pp.127.1.230;
RA   Kumar A., Ellis B.E.;
RT   "The phenylalanine ammonia-lyase gene family in raspberry. Structure,
RT   expression, and evolution.";
RL   Plant Physiol. 127:230-239(2001).
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   -!- DEVELOPMENTAL STAGE: Early fruit ripening.
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; AF237954; AAF40223.1; -; mRNA.
DR   AlphaFoldDB; Q9M568; -.
DR   SMR; Q9M568; -.
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..710
FT                   /note="Phenylalanine ammonia-lyase 1"
FT                   /id="PRO_0000215418"
FT   ACT_SITE        102
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         481
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         197
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        196..198
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   710 AA;  77746 MW;  8ED569D63C0D5167 CRC64;
     MEFYKNGNGA VESFCEGHDP LNWNMAAESL KGSHVDELKR MVSDYRKPVV KLGGETLTIG
     QVAAIASHDG GVRVELSEEK RAGVKASSDW VMDSMGKGTD SYGVTTGFGA TSHRRTKNGG
     ALQRELIRFL NAGIFGSSLD STHKLPHTAT RAAMLVRFNT LLQGYSGIRF EILEAITKFL
     NGNITPCLPL RGTITASGDL VPLSYIAGLL IGRPNSKSVG PKGETLSPAE GFKLAGIDGG
     FFELQPKEGL ALVNGTAVGS GMASMVLFDA NTLAVLSEVM SAIFAEVMQG KPEFTDHLTH
     KLKHHPGQIE AAAIMEHILE GSSYVKEAKK VHEMDPLQKP KQDRYALRTS PQWLGPQIEV
     IRAATKMIER EINSVNDNPL IDVSRNKALH GGNFQELPIG VAMDNTRLAI ASIGKLIFAQ
     FSELVNDYYN NGLPSILTGS SNPSLDYGFK GAEIAMASYC SELQFLANPV TNHVQSAEQH
     NQDVNSLGLI SSRKTSEAVD ILKLMSSTFL VALCQAIDLR HLEENLKIVV KTTVSNVAKR
     TLTVSPNGEL HPSRFSEKDL LTVVDREYLF SYIDDPCLAT YPLMQKLRAE LVEHALKNGE
     RERSANTSIF HKIAAFEEEL KTILPKEVDN ARIEIENGKS EIPNRIKECR SYPLYRFVRE
     ELGTSLLTGE KIKSPGEECY KVFNAICAGK LVDPLLECLK EWNGAPLPIS