ID   PAL1_SOYBN              Reviewed;         713 AA.
AC   P27991;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Phenylalanine ammonia-lyase 1;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL1;
OS   Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. T225; TISSUE=Leaf;
RX   PubMed=1799682; DOI=10.3109/10425179109020788;
RA   Frank R.L., Vodkin L.O.;
RT   "Sequence and structure of a phenylalanine ammonia-lyase gene from Glycine
RT   max.";
RL   DNA Seq. 1:335-346(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; X52953; CAA37129.1; -; Genomic_DNA.
DR   PIR; S22991; S22991.
DR   AlphaFoldDB; P27991; -.
DR   SMR; P27991; -.
DR   STRING; 3847.GLYMA03G33890.1; -.
DR   PRIDE; P27991; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   InParanoid; P27991; -.
DR   SABIO-RK; P27991; -.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0045548; F:phenylalanine ammonia-lyase activity; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..713
FT                   /note="Phenylalanine ammonia-lyase 1"
FT                   /id="PRO_0000215421"
FT   ACT_SITE        105
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         351
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         484
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         200
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        199..201
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   713 AA;  77745 MW;  9D71EF1CC230216A CRC64;
     MEATNGHQNG SFCLSTAKGN NDPLNWGAAA EAMKGSHLDE VKRMVAEYRK PVVRLGGETL
     TIAQVAAVAG HDHGVAVELS ESAREGVKAS SEWVMNSMNN GTDSYGVTTG FGATSHRRTK
     QGGALQKELI RFLNAGIFGN GTESSHTLPH TATRAAMLVR INTLLQGYSG IRFEILEAIT
     KLLNNNVTPC LDLRGTITAS GDLVPLSYIA GLLTGRPNSK AVGPSGEVLN AKEAFELASI
     NSEFFELQPK EGLALVNGTA VGSGLASMVL FEANILAVLS EVLSAIFAEV MQGKPEFTDH
     LTHKLKHHPG QIEAAAIMEH ILDGSSYMKA AKKLHEIDPL QKPKQDRYAL RTSPQWLGPL
     IEVIRFSTKS IEREINSVND NPLIDVSRNK ALHGGNFQGT PIGVSMDNTR LALASIGKLM
     FAQFSELVND FYNNGLPSNL TASRNPSLDY GFKGAEIAMA SYCSELQYLA NPVTTHVQSA
     EQHNQDVNSL GLISSRKTNE AIEILKLMSS TFLIALCQAI DLRHLEENLK NSVKNTVSQV
     SKRILTTGVN GELHPSRFCE KDLLKVVDRE YIFSYIDDPC SATYPLMQKL RQVLVDHALV
     NAECEKDVNS SIFQKIAIFE EELKNLLPKE VEGARAAYES GKAAIPNKIQ ECRSYPLYKF
     VREELGTGLL TGEKVRSPGE EFDKLFTAMC QGKIIDPLME CLGEWNGAPL PIS