ID   PAL1_SOLTU              Reviewed;         720 AA.
AC   P31425;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Phenylalanine ammonia-lyase 1;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL-1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Datura;
RX   PubMed=1541277; DOI=10.1111/j.1432-1033.1992.tb16675.x;
RA   Joos H.J., Hahlbrock K.;
RT   "Phenylalanine ammonia-lyase in potato (Solanum tuberosum L.). Genomic
RT   complexity, structural comparison of two selected genes and modes of
RT   expression.";
RL   Eur. J. Biochem. 204:621-629(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; X63103; CAA44817.1; -; Genomic_DNA.
DR   PIR; S21174; S21174.
DR   AlphaFoldDB; P31425; -.
DR   SMR; P31425; -.
DR   STRING; 4113.PGSC0003DMT400055531; -.
DR   PRIDE; P31425; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   InParanoid; P31425; -.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P31425; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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..720
FT                   /note="Phenylalanine ammonia-lyase 1"
FT                   /id="PRO_0000215419"
FT   ACT_SITE        112
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         491
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         207
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        206..208
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   720 AA;  78618 MW;  BC5BD8FEE43B7F37 CRC64;
     MAPSIAQNGH VNGEVEEVLW KKSIHDPLNW EMAVDSLRGS HLDEVKKMVD EFRKPIVKLW
     GETLTVAQVA SIANADNKTS GFKVELSESA RAGVKASSDW VMDSMSKGTD SYGVTTGFCA
     TSHRRTKNGG ALQKELIKFL NAGVFGNGTE STHTLPHSAT RAAMLVRINT LLQGYSGIRF
     EILEAITKLI NSNITPCLPL RGTVTASGDL VPLSYIAGLL TGRPNSKAVG PSGSKLDADE
     AFRVAAVSGG FFELQPKEGL ALVNGTAVGS GMASIVLYDS NILAVMFEVL SAIFAEVMNG
     KPEFTDYLTH KLKHHPGQIE AAAIMEHILD GSSYVKAAQK LHEMDPLQKP KQDRYALRTS
     PQWLGPQIEV IRAATKMIER EINSVNDNPL IDVSRNKAIH GGNFQGTPIG VSMDNTRLAL
     ASIGKLMFAQ FSELVNDYYN NGLPSNLTAG RNPSLDYGFK GAEIAMASYC SELQFLANPV
     TNHVQSAEQH NQDVNSLGLI SARKTAEAVD ILKLMSSTYL VALCQAIDLR HLEENLKSVV
     KNTVSQVAKR TLTIGAIGEL HPARFCEKEL LRVVDREYLF TYADDPCSST YPLMQKLRQV
     LVDHAMKNGE SEKNINSSIF QKIGAFEDEL NAVLPKEVES ARALLESGNP SIPNRITECR
     SYPLYRLVRQ ELGTELLTGE KVRSPGEEIE KVFTAMCNGQ INDPLLECLK SWNGAPLPIC