ID   PALY_POPTR              Reviewed;         715 AA.
AC   P45730;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL;
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=P.trichocarpa X P.deltoides; TISSUE=Leaf;
RX   PubMed=8108506; DOI=10.1104/pp.102.1.71;
RA   Subramaniam R., Reinold S., Molitor E.K., Douglas C.J.;
RT   "Structure, inheritance, and expression of hybrid poplar (Populus
RT   trichocarpa x Populus deltoides) phenylalanine ammonia-lyase genes.";
RL   Plant Physiol. 102:71-83(1993).
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; L11747; AAA33805.1; -; mRNA.
DR   AlphaFoldDB; P45730; -.
DR   SMR; P45730; -.
DR   STRING; 3694.POPTR_0016s09230.1; -.
DR   PRIDE; P45730; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   UniPathway; UPA00713; UER00725.
DR   ExpressionAtlas; P45730; baseline and differential.
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..715
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215416"
FT   ACT_SITE        107
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         486
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         202
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        201..203
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   715 AA;  77919 MW;  5B9E837A6E8AF2B6 CRC64;
     METVTKNGYQ NGSLESLCVN QRDPLSWGVA AEAMKGSHLD EVKRMVADYR KPVVKLGGET
     LTIAQVASIA GHDTGDVKVE LSESARPGVK ASSDWVMDSM DKGTDSYGVT TGFGATSHRR
     TKQGGALQKE LIRFLNAGIF GNGTETCHTL PHSATRAAML VRINTLLQGY SGIRFEILEA
     ITRLLNNNIT PCLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKATGPTGEV LDAAEAFKAA
     GIESGFFELQ PKEGLALVNG TAVGSGLASM VLFETNVLAV LSELLSAIFA EVMNGKPEFT
     DHLTHKLKHH PGQIEAAAIM EHILDGSAYM KAAKKLHETD PLQKPKQDRY ALRTSPQWLG
     PQIEVIRFST KSIEREINSV NDNPLIDVSR NKAIHGGNFQ GTPIGVSMDN VRLAIASIGK
     LLFAQFSELV NDFYNNGLPS NLTASRNPSL DYGFKGAEIA MASYCSELQY LANPVTTHVQ
     SAEQHNQDVN SLGLISSRKT AEAVDILKLM STTFLVALCQ AIDLRHLEEN LKSAVKNTVS
     QVSKRVLTTG ANGELHPSRF CEKELLKVVD REYVFAYVDD PCSATYPLMQ KLRQVFVDHA
     LENGENEKNF STSVFQKIEA FEEELKALLP KEVESARAAY DSGNSAIDNK IKECRSYPLY
     KFVREELGTV LLTGEKVQSP GEEFDKVFTA MCQGKIIDPM LECLGEWNGS PLPIC