ID   PAL2_PHAVU              Reviewed;         712 AA.
AC   P19142;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Phenylalanine ammonia-lyase class 2;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
DE   AltName: Full=Phenylalanine ammonia-lyase class II;
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; S04127; S04127.
DR   AlphaFoldDB; P19142; -.
DR   SMR; P19142; -.
DR   STRING; 3885.XP_007144370.1; -.
DR   eggNOG; KOG0222; Eukaryota.
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..712
FT                   /note="Phenylalanine ammonia-lyase class 2"
FT                   /id="PRO_0000215410"
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;  77353 MW;  BF31273627288E1D CRC64;
     MDATPNGKDA FVVTAANAAG DPLNWAAAAE ALSGSHLDEV KRMVAEYRKP AVRLGGQTLT
     IAQVAATAAH DQGLKVELAE SARACVKAIS DWVMESMDKG TDSYGITTGF GATSHRRTKQ
     GGALQKELIR FLNAGIFGNG TESNCTLPHT ATRAAMLVRV NTLLQGYSGI RFEILEAITK
     LLNNNITPCL PLRGTITASG DLVPLSYIAG LLTGRPNSKA VGPSGEILNA KEAFELANIG
     SEFFELQPKE GLALVNGTAV GSGLASIVLF EANILAVLSE VISAIFAEVM QGKPEFTDHL
     THKLKHHPGQ IEAAAIMEHI LDGSSYIKAA KKLHEIDPLQ KPKQDRYALR TSPQWLGPQI
     EVIRFSTKSI EREINSVNDN PLISVSRNKA LHGGNFQGTP IGVSMDNTRL AIASIGKLMF
     AQFSDLVNDY YNNGLPSNLT ASRNPSLDYG FKGAEIAMAS YCSELQYLAN PVTSHVQSAE
     QHNQDVNSLG LISSRKTNEA LEILKLMSST FLVALCQAID LRHLEENLKN TVKNVVSQVA
     KRTLTTGVNG ELHPSRFCEK ALLKVVEREY TFAYIDDPCS GTYPLMQKLR QVLVDYALAN
     GENEKNLNTS IFQKIASFEE ELKTLLPKEV EGARLAYEND QCAIPNKIKD CRSYPLYKFV
     REELGTSLLT GEKVISPGEE CDKVFSAMCQ GKIIDPLLEC LGEWNGAPLP IC