ID   PAL1_PHAVU              Reviewed;         506 AA.
AC   P07218;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Phenylalanine ammonia-lyase class 1;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
DE   AltName: Full=Phenylalanine ammonia-lyase class I;
DE   Flags: Fragment;
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 [MRNA].
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16593613; DOI=10.1073/pnas.82.20.6731;
RA   Edwards K., Cramer C.L., Bolwell G.P., Dixon R.A., Schuch W., Lamb C.J.;
RT   "Rapid transient induction of phenylalanine ammonia-lyase mRNA in elicitor-
RT   treated bean cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6731-6735(1985).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33770.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M11939; AAA33770.1; ALT_INIT; mRNA.
DR   PIR; S04129; S04129.
DR   AlphaFoldDB; P07218; -.
DR   SMR; P07218; -.
DR   STRING; 3885.XP_007162756.1; -.
DR   PRIDE; P07218; -.
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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT   CHAIN           <1..506
FT                   /note="Phenylalanine ammonia-lyase class 1"
FT                   /id="PRO_0000215409"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   CONFLICT        20
FT                   /note="V -> E (in Ref. 2; AAA33770)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   506 AA;  55853 MW;  97D14CE431F5D05E CRC64;
     YIAGLLTGRP NSKAVGPSGV VLTAKQAFEL ANINSEFYEL QPKEGLALVN GTAVGSGMAS
     IVLFDANILA VLSEVLSAIF AEVMQGKPEF TDHLTHKLKH HPGQIEAAAI MEHILDGSSY
     MKDAKKLHEI DPLQKPKQDR YALRTSPQWL GPLIEVIRFS TKSIEREINS VNDNPLIDVS
     RNKALHGGNF QGTPIGVSMD NTRLALASIG KLMFAQFSEL VNDFYNNGLP SNLTASRNPS
     LDYGFKGAEI AMASYCSELQ YLANPVTSHV QSAEQHNQDV NSLDLISARK TNESIEILKL
     MSSTFLMGLC QAIDLRHLEE NLKSSVKNTV SQVSKRTLTT GGNGELHPSR FCEKDLLKVV
     DREYVFSYID DPYSGTYPLM QKLRQVLVDH ALINAENEKD VNTSIFQKIA TFEEELKTIL
     PKEVESTRAA YESGKAAIPN KIKECRSYPL YKFVREELGT GLLTGEKVKS PGEEFDKLFT
     AICQGKIIDP LLECLGEWNG APLPIC