ID   PALY_PINTA              Reviewed;         754 AA.
AC   P52777;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL;
OS   Pinus taeda (Loblolly pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3352;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Needle;
RA   Zhang X.H., Chiang V.L.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
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; U39792; AAA84889.1; -; Genomic_DNA.
DR   PIR; T09777; T09777.
DR   AlphaFoldDB; P52777; -.
DR   SMR; P52777; -.
DR   BRENDA; 4.3.1.24; 4861.
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   3: Inferred from homology;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT   CHAIN           1..754
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215412"
FT   ACT_SITE        114
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         387
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         490
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   754 AA;  82600 MW;  59E97746AA0CA398 CRC64;
     MVAAAEITQA NEVQVKSTGL CTDFGSSGSD PLNWVRAAKA MEGSHFEEVK AMVDSYFGAK
     EISIEGKSLT ISDVAAVARR SQVKVKLDAA AAKSRVEESS NWVLTQMTKG TDTYGVTTGF
     GATSHRRTNQ GAELQKELIR FLNAGVLGKC PENVLSEDTT RAAMLVRTNT LLQGYSGVRW
     DILETVEKLL NAWLTPKLPL RGTITASGDL VPLSYIAGLL TGRPNSRVRS RDGIEMSGAE
     ALKKVGLEKP FELQPKEGLA IVNGTSVGAA LASIVCFDAN VLALLSEVIS AMFCEVMNGK
     PEFTDPLTHK LKHHPGQMEA AAIMEYVLDG SSYMKHAAKL HEMNPLQKPK QDRYGLRTSP
     QWLGPQVEII RSATHMIERE INSVNDNPVI DVARDKALHG GNFQGTPIGV SMDNLRLSIS
     AIGKLMFAQF SELVNDYYNG GLPSNLSGGP NPSLDYGLKG AEIAMASYTS ELLYLANPVT
     SHVQSAEQHN QDVNSLGLVS ARKSAEAIDI LKLMLSTYLT ALCQAVDLRH LEENMLATVK
     QIVSQVAKKT LSTGLNGELL PGRFCEKDLL QVVDNEHVFS YIDDPCNASY PLTQKLRNIL
     VEHAFKNAEG EKDPNTSIFN KIPVFEAELK AQLEPQVSLA RESYDKGTSP LPDRIQECRS
     YPLYEFVRNQ LGTKLLSGTR TISPGEVIEV VYDAISEDKV IVPLFKCLDG WKGTLAHSEI
     NNLPRSPLYN DCYDLSPRML LLMLLFSDPE FDWS