ID   PAL1_LITER              Reviewed;         710 AA.
AC   O49835;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Phenylalanine ammonia-lyase 1;
DE            Short=PAL-1;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
OS   Lithospermum erythrorhizon (Purple gromwell) (Lithospermum officinale var.
OS   erythrorhizon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Boraginales; Boraginaceae; Boraginoideae; Lithospermeae;
OC   Lithospermum.
OX   NCBI_TaxID=34254;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9438980; DOI=10.1271/bbb.61.1995;
RA   Yazaki K., Kataoka M., Honda G., Severin K., Heide L.;
RT   "cDNA cloning and gene expression of phenylalanine ammonia-lyase in
RT   Lithospermum erythrorhizon.";
RL   Biosci. Biotechnol. Biochem. 61:1995-2003(1997).
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   -!- TISSUE SPECIFICITY: Expressed mainly in roots.
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; D83075; BAA24928.1; -; mRNA.
DR   PIR; JC5872; JC5872.
DR   AlphaFoldDB; O49835; -.
DR   SMR; O49835; -.
DR   PRIDE; O49835; -.
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..710
FT                   /note="Phenylalanine ammonia-lyase 1"
FT                   /id="PRO_0000215395"
FT   ACT_SITE        102
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         254
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         378
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         481
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         197
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        196..198
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   710 AA;  77518 MW;  CEF1D64B3A80ED03 CRC64;
     METIVENGNG KTMEFCMKDP LNWEMASESM KGSHLDEVKN MVAEFRKPVV QLAGKTLTIG
     QVAAIAARDD GVTVELAEAA REGVKASSDW VMDSMNKGTD SYGVTTGFGA TSHRRTKQGG
     ALQKELIRFL NAGIFGNGTE TSHTLPHSAT RAAMLVRINT LLQGYSGIRF EILEAITKFL
     NTNITPCLPL RGTITASGDL VPLSYIAGLL TGRPNSKAVG PTGEKINAEE AFRLAGISTG
     FFELQPKEGL ALVNGTAVGS GMASMVLYEA NILAVLSEVI SAIFAEVMNG KPEFTDHLTH
     KLKHHPGQIE AAAIMEHILD GSGYVKAAQK LHEMDPLQKP KQDRYALRTS PQWLGPQIEV
     IRSATKMIER EINSVNDNPL IDVSRNKALH GGNFQGTPIG VAMDNTRLAI ASIGKLLFAQ
     FSELVNDYYN NGLPSNLTGS RNPSLDYGFK GAEIAMASYC SELQFLANPV TNHVQSAEQH
     NQDVNSLGLI SSRKTSEAVE ILKLMSSSFL VALFQAVDLR HIEENVRLAV KNTVSQVAKR
     TLTTGVNGEL HPSRFSEKDL LRVVDREYVF AYADDPCLTT YPLMQKLRET LVGHALDNGE
     NEKDVNTSIF HKIAIFEEEL KAILPKEVEN ARASVENGIP AISNRIEECR SYPLYKFVRE
     ELGTELLTGE KVRSPGEELD KVFTAMCEGK LVDPLLACLE AWNGAPLPIC