ID   PALY_TRIMT              Reviewed;         719 AA.
AC   X2BTY5;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Phenylalanine ammonia-lyase {ECO:0000303|PubMed:23801251};
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:A0A4Y6HUI7};
DE   AltName: Full=TmPAL {ECO:0000303|PubMed:23801251};
GN   Name=PAL {ECO:0000303|PubMed:23801251};
OS   Tricholoma matsutake (Matsutake mushroom) (Tricholoma nauseosum).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomataceae; Tricholoma.
OX   NCBI_TaxID=40145 {ECO:0000312|EMBL:ADR32206.1};
RN   [1] {ECO:0000312|EMBL:ADR32206.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=23801251; DOI=10.4014/jmb.1303.03064;
RA   Yoon H., You Y.H., Kim Y.E., Kim Y.J., Kong W.S., Kim J.G.;
RT   "Cloning and mRNA expression analysis of the gene encoding phenylalanine
RT   ammonia-lyase of the ectomycorrhizal fungus Tricholoma matsutake.";
RL   J. Microbiol. Biotechnol. 23:1055-1059(2013).
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   -!- DEVELOPMENTAL STAGE: Very lowly expressed in mycelia, expression is
CC       higher in the primordium and fruiting body (PubMed:23801251). In the
CC       fruiting body, expression is highest in the stipe, followed by the
CC       pileus and gills (PubMed:23801251). {ECO:0000269|PubMed:23801251}.
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; GU980196; ADR32206.1; -; mRNA.
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..719
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000454793"
FT   ACT_SITE        95
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         490
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         201
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   CROSSLNK        200..202
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   719 AA;  77238 MW;  A2A9F4A7D11CAEF7 CRC64;
     MSLLLNGSVN GIPHSKPYNY STLLSRFIES YNELQSYKSG KAVKVDGRTL SVAAVTAAAR
     YHASVELDDC PTARARLAKS RKVITDKVES GTSVYGLSTG FGGSADTRTD QPLLLGHALL
     QHQHMGVLPS SSQALDVLPL LDPNSSTTMP ESWVRGAMLI RMNSLIRGHS GVRWELIEKI
     NEVLSANVTP VVPLRGSISA SGDLSPLSYI AGTLVANPAI RVYHGPAAYG ARQTSPSSDA
     LTQYNIEPLP LASKEHLGIL NGTAFSASVA SLALNDAVHL SLLAQVCTAM GTEALAGTRG
     SYDPFIHATA RPHPGQQIEA AHNIFTLLEE SKLARLHETE VNIHDDQYSL RQDRYPLRTA
     PQFLGPQIED ILSALVAITQ ECNSTTDNPL VDGETGEVHH GGNFQAMAVT NAMEKTRLAL
     HHIGKLLFAQ STELVNPTMN NGLPPSLAAT DPSLNYHAKG IDIATAAYVA ELGYLATPVS
     THIQSAEMHN QAVNSLALIS ARATLNSLEV LSILMASYIY ILCQALDLRA LQSEFVSGLK
     NIINDELVSI FGSFLSASQE DTLSKKLLTI MKSSLEKTTT MDGVDQMLAT AASTTTAFVD
     FFGSSEFTDA SLLGSVVALI SHFRSQVASR AANLLDQLRR DFLSGERGLA PASSYMGKTR
     LLYEFVRVTL GVRMHGSENY ARFVNGLGVE DVSIGQNISL IHEAIRDGKM QPIVASLFT