ID   PALY_WHEAT              Reviewed;         700 AA.
AC   Q43210;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RA   Liao Y.-C., Li H.-P., Kreuzaler F., Fischer R.;
RT   "Nucleotide sequence of one of two tandem genes encoding phenylalanine
RT   ammonia-lyase in Triticum aestivum.";
RL   (er) Plant Gene Register PGR96-102(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; X99705; CAA68036.1; -; Genomic_DNA.
DR   PIR; T06545; T06545.
DR   AlphaFoldDB; Q43210; -.
DR   SMR; Q43210; -.
DR   STRING; 4565.Traes_2AL_9EC3226F7.1; -.
DR   PRIDE; Q43210; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   BRENDA; 4.3.1.24; 6500.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q43210; baseline and differential.
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; 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;
KW   Reference proteome.
FT   CHAIN           1..700
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215428"
FT   ACT_SITE        93
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         332
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         471
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         187
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        186..188
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   700 AA;  75938 MW;  56EE37B4E74E20B5 CRC64;
     MACAWRSRSR ADPLNWGKAA EELSGSHLEA VKRMVEEYRK PVVTMEGATT IAMVAAVAAG
     SDTRVELDES ARGRVKESSD WVMNSMMNGT DSYGVTTGFG ATSHRRTKEG GALQRELIRF
     LNAGAFGTGT DGHVLPAAAT RAAMLVRVNT LLQGYSGIRF EILETIATLL NANVTPCLPL
     RGTITASGDL VPLSYIAGLV TGRPNSMATA PDGSKVNAAE AFKIAGIQHG FFELQPKEGL
     AMVNGTAVGS GLASMVLFEA NVLSLLAEVL SGVFCEVMNG KPEFTDHLTH KLKHHPGQIE
     AAAIMEHILE GSSYMMLAKK LGELDPLMKP KQDRYALRTS PQWLGPQIEV IRAATKSIER
     EINSVNDNPL IDVSRGKAIH GGNFQGTPIG VSMDNTRLAI AAIGKLMFAQ FSELVNDFYN
     NGLPSNLSGG RNPSLDYGFK GAEIAMASYC SELQFLGNPV TNHVQSAEQH NQDVNSLGLI
     SSRKTAEAID ILKLMSSTFL VALCQAIDLR HLEENVKNAV KSCVKTVARK TLSTDNNGHL
     HNARFCEKDL LLTIDREAVF AYADDPCSAN YPLMQKMRAV LVEHALANGE AEAHVETSVF
     AKLAMFEQEL RAVLPKEVEA ARSAVENGTA AQQNRIAECR SYPLYRFVRK ELGTEYLTGE
     KTRSPGEEVD KVFVAMNQGK HIDALLECLK EWNGEPLPLC