ID   PALY_DIGLA              Reviewed;         713 AA.
AC   O23924;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
OS   Digitalis lanata (Grecian foxglove).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Plantaginaceae; Digitalideae; Digitalis.
OX   NCBI_TaxID=49450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Thoeringer C.;
RL   Submitted (NOV-1997) 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; AJ002221; CAA05251.1; -; mRNA.
DR   AlphaFoldDB; O23924; -.
DR   SMR; O23924; -.
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..713
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215391"
FT   ACT_SITE        104
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         484
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         199
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        198..200
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   713 AA;  77733 MW;  747CE64C65BDCC6A CRC64;
     MAAVVENGHH GNNGFCVKQN DPLNWVAAAE ELKGSHLDEV KRMVEEFRKT VVKLGGETLT
     ISQVAAIAAR DNEVAVQLAE SSRAGVKASS DWVMESMNKG TDSYGVTTGF GATSHRRTKQ
     GGALQKELIR FLNAGIFGNG TESTHTLPHS ATRAAMLVRI NTLLQGYSGI RFEILETITK
     FLNHNITPCL PLRGTITASG DLVPLSYIAG LLTGRPNSKA VGPNGESLNA EQAFKLAGAN
     SGLFFELQPK EGLALVNGTA VGSGLASIAL YEANILSLLA EVMSAVFAEV MNGKPEFTDH
     LTHKLKHHPG QIEAAAIMEH ILDGSSYVKA AQKMHEMDPL QKPKQDRYAL RTSPQWLGPQ
     IEVIRTATKM IEREINSVND NPLIDVSRNK ALHGGNFQGT PIGVSMDNSR LAIASIGKLM
     FAQFSELVND FYNNGLPSNL SGGRNPSLDY GFKGSEIAMA SYCSELQFLA NPVTNHVQSA
     EQHNQDVNSL GLISSRKTVE ALDILKLMSS TYLVALCQAI DLRHLEENLR LSVKNTISQV
     AKRTLTTGVN GELHPSRFCE LDLLRVVDRE YVFAYVDDPC SATYPLMQKL RQVLVEHALK
     NGENEKNAST SIFQKIEAFE AELKAVLPKE VESARVALED GKPAIANRIT ECRSYPLYKF
     IREELGTNFL TGEKVMSPGE ECDRVFTAMS KGLIVDPLLK CLEGWNGAPL PIC