ID   PALY_MEDSA              Reviewed;         725 AA.
AC   P27990;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
OS   Medicago sativa (Alfalfa).
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; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Apollo;
RX   PubMed=1715786; DOI=10.1007/bf00040636;
RA   Gowri G., Paiva N.L., Dixon R.A.;
RT   "Stress responses in alfalfa (Medicago sativa L.) 12. Sequence analysis of
RT   phenylalanine ammonia-lyase (PAL) cDNA clones and appearance of PAL
RT   transcripts in elicitor-treated cell cultures and developing plants.";
RL   Plant Mol. Biol. 17:415-429(1991).
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; X58180; CAA41169.1; -; mRNA.
DR   PIR; S17444; S17444.
DR   AlphaFoldDB; P27990; -.
DR   SMR; P27990; -.
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..725
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215400"
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;  78866 MW;  19906A2575F64D7D CRC64;
     METISAAITK NNANESFCLI HAKNNNNMKV NEADPLNWGV AAEAMKGSHL DEVKRMVAEY
     RKPVVRLGGE TLTISQVAAI AAHDHGVQVD LSESARDGVK ASSEWVMESM NKGTDSYGVT
     TGFGATSHSR TKQGGALQKE LIRFLNAGIF GNGTESNHTL PKTATRAAML VRINTLLQGY
     SGIDFEILEA ITKPLNKTVT PCLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKAHGPSGEV
     LNAKEAFNLA GINAEFFELQ PKEGLALVNG TAVGSGLASI VLFEANILAV LSEVLSAIFA
     EVMQGKPEFT DHLTHKLKHH PGQIEAAAIM EHILDGSSYV KAAKKLHEID PLQKPKQDRY
     ALRTSPQWLG PLVEVIRFST KSIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVSMDN
     TRLALASIGK LMFAQFSELV NDFYNNGLPS NLSASRNPSL DYGFKGAEIA MASYCSELQY
     LANPVTTHVQ SAEQHNQDVN SLGLISARKT NEAIEILQLM SSTFLIALCQ AIDLRHLEEN
     LKNSVKNTVS QVAKKTLTMG VNGELHPSRF CEKDLLKVVD REHVFAYIDD PCSATYPLSQ
     KLRQVLVDHA LVNGESEKNF NTSIFQKIAT FEEELKTLLP KEVESARTAY ESGNPTIPNK
     INGCRSYPLY KFVREELGTG LLTGENVISP GEECDKLFSA MCQGKIIDPL LECLGEWNGA
     PLPIC