ID   PALY_TRISU              Reviewed;         725 AA.
AC   P45734;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL1;
OS   Trifolium subterraneum (Subterranean clover).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX   NCBI_TaxID=3900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Karridale; TISSUE=Leaf;
RX   PubMed=8125321; DOI=10.1016/0378-1119(94)90786-2;
RA   Howles P.A., Arioli T., Weinman J.J.;
RT   "Characterization of a phenylalanine ammonia-lyase multigene family in
RT   Trifolium subterraneum.";
RL   Gene 138:87-92(1994).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M91192; AAA17993.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P45734; -.
DR   SMR; P45734; -.
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   3: Inferred from homology;
KW   Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT   CHAIN           1..725
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215426"
FT   ACT_SITE        117
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         393
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         496
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         212
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        211..213
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   725 AA;  78998 MW;  70F9925C86622240 CRC64;
     MEVVAAAILK NNINDYDSFC LTHANANNMK VNAADPLNWG VAAEAMKGSH LDEVKRMVEE
     YRKPVVRLGG ETLTISQVAA IAAHDGATVE LSESARAGVK ASSDWVMESM NKGTDSYGVT
     TGFGATSHRR TKQGGALQKE LIRFLNAGIF GNGTESNHTL PHTATRAAML VRINTLLQGY
     SGIRFEILEA ITKLLNNNIT PCLPLRGTIT ASGDLVPLSY IAGLLTGRSN SKAHGPSGEM
     LNAKEAFQLA GINAEFFELQ PKEGLALVNG TAVGSGLASI VLFEANILAV LSEVLSAIFA
     EVMQGKPEFT DHLTHKLKHH PGQIEAAAIM EHILHGSAYV KDAKKLHEMD PLQKPKQDRY
     ALRTSPQWLG PLIEVIRFST KSIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVSMDN
     TRLALASIGK LLFAQFSELV NDFYNNGLPS NLSASRNPSL DYGFKGSEIA MASYCSELQY
     LANPVTTHVQ SAEQHNQDVN SLGLISSRKT KEAIEILQLM SSTFLIALCQ AIDLRHLEEN
     LKNSVKNTVS QVAKKTLTIG VSGELHPSRF CEKDLLKVVD REHVFSYIDD PCSATYPLAQ
     KLRQVLVDHA LVNGESEKNS NTSIFQKIAT FEEELKTLLP KEVESARTAY ENGNSTIANK
     INGCRSYPLY KFVREELGTS LLTGERVISP GEECDKLFTA MCQGKIIDPL LKCLGEWNGA
     PLPIC