ID   PAL2_IPOBA              Reviewed;         708 AA.
AC   Q42858;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
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].
RC   STRAIN=cv. Beniazuma; TISSUE=Root;
RA   Tanaka Y.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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; D78640; BAA11459.1; -; mRNA.
DR   PIR; T10909; T10909.
DR   AlphaFoldDB; Q42858; -.
DR   SMR; Q42858; -.
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..708
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215394"
FT   ACT_SITE        100
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         340
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         479
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         195
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        194..196
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   708 AA;  77383 MW;  C10F736C41F1BEC6 CRC64;
     MEGAIANGHT NDFCIKVDPL NWEMAADSLK GSHLDEVKRM VAEFRNPAVK IGGQTLTSLR
     SPPIAARDNA SKWSSPRLPA RRESSSDWVM NSMNNGTDSY GVTTGFGATS HRRTKNGHAL
     QQELIRFLNA GIFGTGTGAS HTLPHSATRA AMLVRINTLL QGYSGIRFEI LEAITKLLNH
     NITPCLPLRG TITASGDLVP LSYIAGLLTG RPNSKAVGPN GEALTAEEAF KLAGVQGGFF
     ELQPKEGLAL VNGTAVGSGM ASMVLFEANV LAVLSEVLSA IFAEVMNGKP EFTDHLTHKL
     KHHPGQIEAA AIMEHILDRS YYMKAAQKLH EMDPLQKPKQ DRYALRTSPQ WLGPQIEVIR
     QATKMIEREI NSVNDNPLID VSRNKALHGG NFQGTPIGVS MDNSRLALAS IGKLIFAQFS
     ELVNDYYNNG LPSNLTAGRN PSLDYGFKGV EIAMASYCSE LQFLANPVTN HVQSAEQHNQ
     DVNSLGLISA RKTAEAVDVL KLMSSTYLVA LCQAIDLRHL EENLKNAVRN TVNQVAKRTL
     TMGVNGELHP SRFCEKDLLR VVDREYVFAY ADDPCSANYP LFQKLRQVLV DHALQNGEHE
     KNVSTSIFQK IAAFEDELKA VLPKEVEGAR SAIENGNPAI PNRITECRSY PLYKFVREEL
     GTEMLTGEKV KSPGEVCDKV FTAVCDGGII DPLLECLKSW DGAPLPIC