ID   PALY_RHOMI              Reviewed;         713 AA.
AC   P10248;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Phenylalanine ammonia-lyase {ECO:0000303|PubMed:3205749};
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:A0A4Y6HUI7};
GN   Name=PAL;
OS   Rhodotorula mucilaginosa (Yeast) (Rhodotorula rubra).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL Y-15597;
RX   PubMed=3205749; DOI=10.1093/nar/16.23.11381;
RA   Filpula D., Strausberg R.L., Vaslet C.A., Sykes A., Levy A.;
RT   "Nucleotide sequence of gene for phenylalanine ammonia-lyase from
RT   Rhodotorula rubra.";
RL   Nucleic Acids Res. 16:11381-11381(1988).
RN   [2]
RP   GENE STRUCTURE.
RC   STRAIN=NRRL Y-15597;
RX   PubMed=3205750; DOI=10.1093/nar/16.23.11382;
RA   Filpula D., Strausberg R.L., Vaslet C.A., Sykes A., Levy A.;
RT   "cDNA and genomic cloning of yeast phenylalanine ammonia-lyase genes reveal
RT   genomic intron deletions.";
RL   Nucleic Acids Res. 16:11382-11382(1988).
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; X13094; CAA31486.1; -; Genomic_DNA.
DR   PIR; S01999; S01999.
DR   AlphaFoldDB; P10248; -.
DR   SMR; P10248; -.
DR   BRENDA; 4.3.1.24; 5433.
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   3: Inferred from homology;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT   CHAIN           1..713
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215431"
FT   ACT_SITE        116
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         362
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         399
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         501
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         218
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        217..219
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   713 AA;  76001 MW;  6EB8317CBB037D88 CRC64;
     MAPSVDSIAT SVANSLSNGL HAAAAANGGD VHKKTAGAGS LLPTTETTQL DIVERILADA
     GATDQIKLDG YTLTLGDVVG AARRGRSVKV ADSPHIREKI DASVEFLRTQ LDNSVYGVTT
     GFGGSADTRT EDAISLQKAL LEHQLCGVLP TSMDGFALGR GLENSLPLEV VRGAMTIRVN
     SLTRGHSAVR IVVLEALTNF LNHGITPIVP LRGTISASGD LSPLSYIAAS ITGHPDSKVH
     VDGKIMSAQE AIALKGLQPV VLGPKEGLGL VNGTAVSASM ATLALTDAHV LSLLAQALTA
     LTVEAMVGHA GSFHPFLHDV TRPHPTQIEV ARNIRTLLEG SKYAVHHETE VKVKDDEGIL
     RQDRYPLRCS PQWLGPLVSD MIHAHAVLSL EAGQSTTDNP LIDLENKMTH HGGAFMASSV
     GNTMEKTRLA VALMGKVSFT QLTEMLNAGM NRALPSCLAA EDPSLSYHCK GLDIAAAAYT
     SELGHLANPV STHVQPAEMG NQAINSLALI SARRTAEAND VLSLLLATHL YCVLQAVDLR
     AMEFEHTKAF EPMVTELLKQ HFGALATAEV EDKVRKSIYK RLQQNNSYDL EQRWHDTFSV
     ATGAVVEALA GQEVSLASLN AWKVACAEKA IALTRSVRDS FWAAPSSSSP ALKYLSPRTR
     VLYSFVREEV GVKARRGDVY LGKQEVTIGT NVSRIYEAIK SGCIAPVLVK MMA