ID   PAL1_DAUCA              Reviewed;         708 AA.
AC   O23865;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Phenylalanine ammonia-lyase 1;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL1;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Kurodagosun;
RX   PubMed=9337617; DOI=10.1111/j.1751-1097.1997.tb03174.x;
RA   Takeda J., Ozeki Y., Yoshida K.;
RT   "Action spectrum for induction of promoter activity of phenylalanine
RT   ammonia-lyase gene by UV in carrot suspension cells.";
RL   Photochem. Photobiol. 66:464-470(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   -!- 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; D85850; BAA23367.1; -; Genomic_DNA.
DR   PIR; T14295; T14295.
DR   AlphaFoldDB; O23865; -.
DR   SMR; O23865; -.
DR   PRIDE; O23865; -.
DR   EnsemblPlants; KZM91802; KZM91802; DCAR_020833.
DR   Gramene; KZM91802; KZM91802; DCAR_020833.
DR   OMA; VEDHATQ; -.
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..708
FT                   /note="Phenylalanine ammonia-lyase 1"
FT                   /id="PRO_0000215390"
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;  76845 MW;  0610411373E680E3 CRC64;
     MDCENKNVVL GNGLCMQKDP LNWGMAAEAL TGSHLDEVKR MVAEFRKPMV QLGGETLTVS
     QVAAIAAGSV KVELAESARA GVKASSDWVM ESMNKGTDSY GVTTGFGATS HRRTKQGGAL
     QKELIRFLNA GIFGSGNDSS NILPHSATRA AMLVRINTLL QGYSGIRFEI LEAITKFLNQ
     NITPCLPLRG TITASGDLVP LSYIAGLLTG RPNSKAVGPT GENLTAAEAF KLAGVDGGFF
     ELQPKEGLAL VNGTAVGSGM ASMVLFETNI LAVLAEVMSA IFAEVMQGKP EFTDHLTHKL
     KHHPGQIEAA AIMEHILDGS SYVKAAEKQH EMDPLQKPKQ DRYALRTSPQ WLGPQIEVIR
     SSTKMIEREI NSVNDNPLID VSRNKAIHGG NFQGTPIGVS MDNTRLAIAA IGKLMFAQFS
     ELVNDFYNNG LPSNLSGGRN PSLDYGFKGA EIAMASYCSE LQFLGNPVTN HVQSAEQHNQ
     DVNSLGLISS RKTAEAVEIL KLMSTTFLVG LCQAVDLRHL EENLKSTVKN TVSQVAKKVL
     TMGVNGELHP SRFCELDLLR VVDREYIFAY IDDPCSATYP LMQKLRQVLV EHALKNGETE
     KNLSTSIFQK IAAFEDELKA LLPKEVESAR AVVESGNPAI PNRIKECRSY PLYKFIREEL
     GTVYLTGEKV TSPGEEFDKV FTAMSKGEII DPLLACLESW NGAPLPIA