ID   PAL1_POPKI              Reviewed;         682 AA.
AC   P45731;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Phenylalanine ammonia-lyase G1;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PALG1; Synonyms=PAL;
OS   Populus kitakamiensis (Aspen) (Populus sieboldii x Populus grandidentata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=34292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7548831; DOI=10.1007/bf00032674;
RA   Osakabe Y., Osakabe K., Kawai S., Katayama Y., Morohoshi N.;
RT   "Characterization of the structure and determination of mRNA levels of the
RT   phenylalanine ammonia-lyase gene family from Populus kitakamiensis.";
RL   Plant Mol. Biol. 28:1133-1141(1995).
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; D30657; BAA06337.1; -; Genomic_DNA.
DR   AlphaFoldDB; P45731; -.
DR   SMR; P45731; -.
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..682
FT                   /note="Phenylalanine ammonia-lyase G1"
FT                   /id="PRO_0000215413"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         453
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         169
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        168..170
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   682 AA;  74522 MW;  F32874E942174155 CRC64;
     MAADSLKGSH LDEVKRMIEE YRNPVVKLGG ETLTIGQVTA IASGHVGVMV ELSEEARAGV
     KASNDWVMDS KNSHAVTAGF GATSHRKTKQ GGELQKELIR FLNVGIFGNG TESNHILPRS
     ATRAAMLVRT NTLLQGYSGI RFEMLEAITK LLNHNITPCL PLRGTITASG DLVPLAYIAG
     LLTGRHNSKA VGPNGEPLTS TEAFTQAGIN GGFFELQPKE GLALVNGTAV GSGLASMVLF
     EANVLAILSE VLSAIFAEVM QGKPEFTDHL THKLKHHPGQ IEAAAIMEHI LDGSAYVKEA
     QKLLEIDPLQ KPKQDRYALR TSPQWLGPLI EVIRTSTKMI EREINSVNDN PLIDVSRSKA
     LQGGNFQGTP IGVSMDNTRL AIASIGKLMF AQFSELVNDF YNNGLPSNLT GGRNPSLDYG
     FKGAEIAMAS YCSELQFLAN PVTNHVQSAE QHNQDVNSLG LISSRKTAEA VDILKLMSTT
     FLVGLCQAVD LRHIEENLKN TVKNTVSQVA KRVLTMGFNG ELHPSRLCEK DLLKLVDKEH
     VFAYIDDPCS ATYPLMQKLR QVLVEHALVN GERETNSTTS IFQKIRSFEE ELKTLLPKEV
     ESARLEVENG NPVVPNRIKE CRSYPLYKFV REELGTSLLT GEKVKSPGED FDKVFTAICA
     GKLMDPLLEC LKEWNGAPLP IC