ID   PAL1_IPOBA              Reviewed;         707 AA.
AC   P14166;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, 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};
GN   Name=PAL;
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16666943; DOI=10.1104/pp.90.4.1403;
RA   Tanaka Y., Matsuoka M., Yamanoto N., Ohashi Y., Kano-Murakami Y., Ozeki Y.;
RT   "Structure and characterization of a cDNA clone for phenylalanine ammonia-
RT   lyase from cut-injured roots of sweet potato.";
RL   Plant Physiol. 90:1403-1407(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   EMBL; M29232; AAA33389.1; -; mRNA.
DR   PIR; S29029; S29029.
DR   AlphaFoldDB; P14166; -.
DR   SMR; P14166; -.
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..707
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215393"
FT   ACT_SITE        98
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         478
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         193
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        192..194
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   707 AA;  77138 MW;  87B9513A91228FBB CRC64;
     MANQNGFCIK KQQVDPLNWE MAAESLRGSH LDEVKRMVAE FRKPAVKLGG ETLTVAQVAR
     IASRDNAVAV ELSEEARAGV KASSDWVMDS MNKGTDSYGV TTGFGATSHR RTKQGGALQK
     ELIRFLNAGI FGNATESCHT LPHSATRAAM LVRINTLLQG YSGIRFEILE AITKLLNHNI
     TPCLPLRGTI TASGDLVPLS YIAGLITGRP NSKAVGPNGE TLNAEEALRL SRSGRRIFRV
     ASPRKGLPSL MAPPLVLGMA SMVLFEANVL AVLSEVLSAI FAEVMNGKPE FTDHLTHKLK
     HHPGQIEAAA IMEHILDGSS YVKAAQKLHE MDPLQKPKQD RYALRTSPQW LGPQIEVIRA
     ATKMIEREIN SVNDNPLIDV ARSKALHGGN FQGTPIGVSM DNSRLALASI GKLLFAQFSE
     LVNDYYNNGL PSNLTAGRNP SLDYGFKGAE IAMASYCSEL QFLANPVTNH VQSAEQHNQD
     VNSLGLISAR KTAEAVDVLK LMSSTYLVAL CQAIDLRFLE ENLRNAVKNA VTQVAKRTLT
     VGANGELHPA RFCEKDLLRV VDREYVFAYA DDPCSANYPL MQKLRQALVD HALQNGENEK
     NTGTSIFLKV AAFEDELKAV LPKEVEAARI AVESGNPAIP NRIKECRSYP LYKFVREGLG
     TELLTGEKVR SPGEECDKVF TAMCEGSIID PLLECLKSWD GAPLPIC