ID   PAL2_PEA                Reviewed;         724 AA.
AC   Q04593;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Phenylalanine ammonia-lyase 2;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL2;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Midoriusui; TISSUE=Epicotyl;
RA   Yamada T., Tanaka Y., Sriprasertsak P., Kato H., Hashimoto T., Kawamata S.,
RA   Ichinose Y., Kato H., Shiraishi T., Oku H.;
RT   "Phenylalanine ammonia-lyase genes from Pisum sativum: structure, organ-
RT   specific expression and regulation by fungal elicitor and suppressor.";
RL   Plant Cell Physiol. 33:715-725(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   -!- TISSUE SPECIFICITY: Present at high levels in roots, with slightly
CC       higher amounts in roots with nodules than those without, and at
CC       moderate levels in stems.
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; D10003; BAA00887.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q04593; -.
DR   SMR; Q04593; -.
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..724
FT                   /note="Phenylalanine ammonia-lyase 2"
FT                   /id="PRO_0000215404"
FT   ACT_SITE        117
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         392
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         495
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         211
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        210..212
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   724 AA;  79009 MW;  72666CF1B1F7BE7F CRC64;
     MEAIGAAITK NNSGYDSFCL TNAKNNNIKV SDSDPLNWGV AAEAMKGSHL DEVKRMVDEY
     RKPVVRLGGE TLTISQVAAI AAHDHGVKVE LSESARAGVK ASSDWVMESM NKGTDSYGVT
     TVHGATSHRR TKQGGALQKE LIRFLNAGIF GNGSESTHTL PHTATRAAML VRINTLLQGY
     SGIRFEILEA ITKLINNNVT PCLLRGTITA SGDLVPLSYI AGLLTGRPNS KAHGPSGEIL
     NAREAFQSAG INDGFFELQP KEGLALVNGT AVGSGLASIV LFEANILAVL SEVLSAIFAE
     VMQGKPEFTD HLTHKLKHHP GQIEAAAIME HILDGSAYVK AAKKLHEMDP LQKPKQDRYA
     LRTSPQWLGP LIEVIRFSTK SIEREINSVN DNPLIDVSRN KALHGGNFQG TPIGVSMDNT
     RLALASIGKL LFAQFSELVN DFYNNGLPSN LSASRNPSLD YGFKGSEIAM ASYCSELQYL
     ANPVTTHVQS AEQHNQDVNS LGLISSRKTY EAIEILQLMS STFLIALCQA IDLRHLEENL
     KNSVKNMVSH VAKRTLTTGI NGELHPSRFC EKDLLRVVDR EHVFSYIDDP CSATYPLMQK
     LRQVLVDHAL VNGESEKNLN TSIFQKIATF EDELKTLLPK EVESARGAYE NGNTTISNKI
     KECRSYPLYK FVREELGTSL LTGEKVISPG EECDKLFTAI CQGKIIDPLL ECLGDWNGAP
     LPIS