ID   PAL3_TOBAC              Reviewed;         712 AA.
AC   P45733;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Samsun NN; TISSUE=Leaf;
RX   PubMed=7824656; DOI=10.1104/pp.106.3.877;
RA   Pellegrini L., Rohfritsch O., Fritig B., Legrand M.;
RT   "Phenylalanine ammonia-lyase in tobacco. Molecular cloning and gene
RT   expression during the hypersensitive reaction to tobacco mosaic virus and
RT   the response to a fungal elicitor.";
RL   Plant Physiol. 106:877-886(1994).
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   -!- INDUCTION: Strongly induced during the hypersensitive reaction to TMV
CC       or to a fungal elicitor.
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; X78269; CAA55075.1; -; mRNA.
DR   PIR; T03663; T03663.
DR   RefSeq; NP_001312473.1; NM_001325544.1.
DR   AlphaFoldDB; P45733; -.
DR   SMR; P45733; -.
DR   STRING; 4097.P45733; -.
DR   GeneID; 107792668; -.
DR   KEGG; nta:107792668; -.
DR   BRENDA; 4.3.1.24; 3645.
DR   SABIO-RK; P45733; -.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000084051; Unplaced.
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   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism;
KW   Reference proteome.
FT   CHAIN           1..712
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215425"
FT   ACT_SITE        104
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         483
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         199
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        198..200
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   712 AA;  77510 MW;  665B5FA0A83244F0 CRC64;
     MAGVAQNGHQ EMDFCVKVDP LNWEMAADSL KGSHLDEVKK MVAEFRKPVV KLGGETLTVA
     QVAAIAAKDN AKTVKVELSE GARAGVKASS DWVMDSMSKG TDSYGVTTGF GATSHRRTKN
     GGALQKELIR FLNAGVFGNG TESCHTLPQS GTRAAMLVRI NTLLQGYSGI RFEILEAITK
     LLNHNVTPCL PLRGTITASG DLVPLSYIAG LLTGRPNSKA IGPNGETLNA EEAFRVAGVN
     SGFFELQPKE GLALVNGTAV GSGLASMVLF DANILAVFSE VLSAIFAEVM NGKPEFTDHL
     THKLKHHPGQ IEAAAIMEHI LDGSSYVKAP QKLHETDPLQ KPKQDRYALR TSPQWLGPQI
     EVIRSATKMI EREINSVNDN PLIDVSRNKA LHGGNFQGTP IGVSMDNARL ALASIGKLMF
     AQFSELVNDY YNNGLPSNLT AGRNPSLDYG FKGSEIAMAS YCSELQFLAN PVTNHVQSAE
     QHNQDVNSLG LISARKTAEA VDILKLMSST YLVALCQAID LRHLEENLRN AVKNTVSQVA
     KRTLTMGANG ELHPSRFCEK DLLRVVDREY VFRYADDACS ANYPLMQKLR QVLVDHALEN
     GENEKNANSS IFQKILAFEG ELKAVLPKEV ESARISLENG NPAIANRIKE CRSYPLYRFV
     REELGAELLT GEKVRSPGEE CDKVFTAMCN GQIIDSLLEC LKEWNGAPLP IC