ID   PAL3_PHAVU              Reviewed;         710 AA.
AC   P19143;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Phenylalanine ammonia-lyase class 3;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
DE   AltName: Full=Phenylalanine ammonia-lyase class III;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Cramer C.L., Edwards K., Dron M., Liang X., Dildine S.L., Bolwell G.P.,
RA   Dixon R.A., Lamb C.J., Schuch W.;
RT   "Phenylalanine ammonia-lyase gene organisation and structure.";
RL   Plant Mol. Biol. 12:367-383(1989).
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   PIR; S04128; S04128.
DR   RefSeq; XP_007142542.1; XM_007142480.1.
DR   AlphaFoldDB; P19143; -.
DR   SMR; P19143; -.
DR   STRING; 3885.XP_007142542.1; -.
DR   EnsemblPlants; ESW14536; ESW14536; PHAVU_008G289500g.
DR   GeneID; 18624368; -.
DR   Gramene; ESW14536; ESW14536; PHAVU_008G289500g.
DR   KEGG; pvu:PHAVU_008G289500g; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   OMA; MVRFLNC; -.
DR   OrthoDB; 923557at2759; -.
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..710
FT                   /note="Phenylalanine ammonia-lyase class 3"
FT                   /id="PRO_0000215411"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         482
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   710 AA;  77939 MW;  C170771F4AE54773 CRC64;
     MATITPQKGS QSEVGVSNTD PLNWGNAVES LKGSHLEEVK GMVAEYREAV IHVGGGETLT
     VSKVAAVANQ YLQAKVDLSE SAREGVDSSC KWIVDNIDKG IPIYGVTTGF GANSNRQTQE
     GLALQKEMVR FLNCAIFGYQ TELSHTLPKS ATRAAMLVRV NTLLQGYSGI RFEILEAITK
     LLNHNVTPIL PLRGTITASG DLIPLSYIAA LLIGRRNSKA VGPSGESLNA KEAFHLAGVD
     GGFFELKPKE GLALVNGTAV GSGVASMVLF EANILALLAE VLSAVFAEVM QGKPEFTDHL
     IHKLKYHPGQ IEAAAIMEHI LDGSSYVKNA KLQQPDPLQK PRKDRYALVT SPQWLGPQIE
     IIRFSTKSIE REINSVNDNP LIDVTRNKAV SGGNFQGTPI GVSMDNARLA VASIGKLIFA
     QFTELANDLY NNGLPSNLSV GRNPSLDYGF KASEVAMAAY CSELQYLANP VTSHVQSTEQ
     HNQDVNSLGL ISALKTVEAI EILKLMSSTY LVALCQAIDL RHLEEIFKNT VKNTVSRVAL
     KTLTTEDKEE TNPFRFSEEE LLKVVDREYV FSYIDDPLNV RYPLMPKLKQ VLYEQAHTSV
     INDKNVSLLV FEKIGAFEDE LKSLLPKEVE SARVAYENGN PATPNRIKEC RSYPLYKFVR
     EELGIRLLTG EKALSPDEEF EKVYTAMCQA KIIDPILECL EDWNGVPIPI