ID   PALY_BROFI              Reviewed;         703 AA.
AC   Q42609;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL;
OS   Bromheadia finlaysoniana (Orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Vandeae; Adrorhizinae; Bromheadia.
OX   NCBI_TaxID=41205;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Liew C.-F., Goh C.-J., Loh C.-S., Lim S.-H.;
RT   "Cloning and nucleotide sequence of a cDNA encoding phenylalanine ammonia-
RT   lyase from Bromheadia finlaysoniana (Lindl.) Rchb.f.";
RL   (er) Plant Gene Register PGR96-087(1996).
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; X99997; CAA68256.1; -; mRNA.
DR   AlphaFoldDB; Q42609; -.
DR   SMR; Q42609; -.
DR   PRIDE; Q42609; -.
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..703
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215386"
FT   ACT_SITE        98
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         372
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         475
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         191
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        190..192
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   703 AA;  76026 MW;  9E848050F97B25AC CRC64;
     MEVSKENGLC LQGRDPLNWG AAAAELQGSH LDEVKKMVEE FRRPVVKLEG VKLKISQVAA
     VAFGGGASAV ELAESARAGV KASSDWVLES VDKGTDSYGV TTGFGATSHR RTKQGGALQK
     ELIKFLNAGI FGSGNSNTLP SAATRAAMLV RINTLLQGYS GIRFEILKAI ATLLNKNITP
     CLPLRGTITA SGDLVPLSYL AGILTGRPNS KARTPNGSTV DATTAFRLAG ISSGFFDLQP
     KEGLALVNGT AVGSGVASIV LFETNILAVM AELLSALFCE VMQGKPEFTD HLTHKLKHHP
     GQIEAAAVME HILEGSSYMK MAKKLHEMDP LQKPKQDRYA LRTSPQWLGP QIEVIRAATK
     SIEREINSVN DNPLIDVSRN KALHGGNFQG TPIGVSMDNT RLAIAAIGKL MFAQFSELVN
     DFYNNGLPSN LSSGRNPSLD YGFKGAEIAM ASYCSELQAL ANPVTNHVQS AEQHNQDVNS
     LGLISSRKTA EAVDILKLMS TTFLVGLCQA VDLRHLEENL KNAVKNTVSQ VAKRVLTMGV
     NGELHPSRFC EKDLIKVIDR EYVFAYADDP CSSTYPLMQK LRAVIVEHAL NNGVKEKDSN
     TSIFQKISSF ENELKAALPK EVEAARAEFE NGSPAIENRI KDCRSYPLYK FVKEVGSGFL
     TGEKVVSPGE EFDKVFNAIC EGKAIDPMLD CLKEWNGAPL PIC