ID   PALY_AMAMU              Reviewed;         740 AA.
AC   O93967;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Phenylalanine ammonia-lyase {ECO:0000303|PubMed:10074091};
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:A0A4Y6HUI7};
GN   Name=PAL;
OS   Amanita muscaria (Fly agaric).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=41956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10074091; DOI=10.1128/jb.181.6.1931-1933.1999;
RA   Nehls U., Ecke M., Hampp R.;
RT   "Sugar- and nitrogen-dependent regulation of an Amanita muscaria
RT   phenylalanine ammonium lyase gene.";
RL   J. Bacteriol. 181:1931-1933(1999).
CC   -!- FUNCTION: Catalyzes the non-oxidative deamination of L-phenylalanine to
CC       form trans-cinnamic acid and a free ammonium ion (By similarity).
CC       Facilitates the commitment step in phenylpropanoid pathways that
CC       produce secondary metabolites such as lignins, coumarins and flavonoids
CC       (By similarity). {ECO:0000250|UniProtKB:A0A4Y6HUI7,
CC       ECO:0000250|UniProtKB:P11544}.
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:A0A4Y6HUI7};
CC   -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC       trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P11544}.
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; AJ010143; CAA09013.1; -; mRNA.
DR   AlphaFoldDB; O93967; -.
DR   SMR; O93967; -.
DR   UniPathway; UPA00713; UER00725.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045548; F:phenylalanine ammonia-lyase activity; ISS:UniProtKB.
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..740
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215430"
FT   ACT_SITE        120
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         511
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         225
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        224..226
FT                   /note="5-imidazolinone (Ser-Gly)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   740 AA;  80157 MW;  B055CFF3D8B7BCEE CRC64;
     MGLDNSKNTA KFFDLPKAVH GMNGTTPVNG FKATALSKAS RTMTKTSALS QFLEAYRELE
     GYKNGRAIKV DGQTLSIAAV AAAARYNAAV ELDESPLVKE RVRKSQLAIA NKVSTGASVY
     GLSTGFGGSA DTRTDKPMLL GFALLQHQHV GILPTSTEPL DVLPLQDANN TSMPEAWIRG
     AILIRMNSLI RGHSGIRWEL IEKMRELLAA NVIPVVPLRG SISSSGDLSP LSYIAGTIIG
     NPSIKVYHGP SKSGIRQIGS SKDVLALHNI EPFPLESKEP LGILNGTAFS ASVAALALNE
     AIHLVLLAQV CTAMGTEALI GTRASHAPFI HATARPHPGQ VECAENIWNL LDGSKLAQLE
     EHEVRLEDDK YTLRQDRYPL RTSPQFLGPQ IEDIISAFQT VTQECNYLPA TDNPLIDGET
     GESHHGGNFQ AMAVTNAMEK TRLALHHVGK LLFSQSTELV NPAMNRGLPP SVAATDPSLN
     YHAKGLDIAT AAYVAEATPG PTHIQSAEMH NQAVNSLALI SARATITSLE VLTSLIASYL
     YILCQALDLR ALQREFLPGL DIIIREELRS SFGSFLSSEQ MEKLQQNLTS AFEDHLDKTT
     TMDNTDRMTT MAATSSSVLL QFFTDSGASV PPSSCDLLSS VSSFQSSVAT RSSVLMDDLR
     KEYIFGDRGP TPASQYIGKT RPVYQFIRTT IGVRKHGSEN YNKFYNGLGV EDVTIGQNIS
     RIYESIRDGK MQSIIVSLFD