ID   PAL4_POPKI              Reviewed;         571 AA.
AC   Q40910;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Phenylalanine ammonia-lyase G4;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
DE   Flags: Fragment;
GN   Name=PALG4;
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; D43803; BAA07861.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q40910; -.
DR   SMR; Q40910; -.
DR   PRIDE; Q40910; -.
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..571
FT                   /note="Phenylalanine ammonia-lyase G4"
FT                   /id="PRO_0000215415"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         57
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        56..58
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   NON_TER         1
SQ   SEQUENCE   571 AA;  62484 MW;  6B76CC92D2DB425F CRC64;
     STHTLPHSAS RAAMLVRINT LLQGYSGIRF EILEAITKLL NHNITPCLPL RGTITASGDL
     VPLSYIAGLL TGRPNSKAVG PNGETMAAAE AFTLAGINGG FFELQPKEGL ALVNGTAVGS
     GLASMVLFET NVLAILSEVL SAIFAEVMQG KPEFTDHLTH KLKHHPGQIE AAAVMEHILD
     GSSYVKAAQK LHEIDPLQKP KQDRYALRTS PQWLGPLIEV IRTSTKMIER EINSVNDNPL
     IDVSRNKALH GGNFPGSPIG VSMDNTLVLA IASIGKLMFA QFSELVNDYY NNGLPSNLTG
     GRNPSLDYGF KGAEIAMASY CSELQFLANP VTNHVQSAEQ HNQDVNSLGL ISARKTAEAV
     EILNVMSTTW LVALCQAIDL RHIEENLKNT VKNTVSQVAK RVLTMGFNGE LHPSRFCEKD
     LLKVVDREYV FTYIDDPCSA TYPLMQKLRQ VLVDHALMNG EKEQNSSTSI FQKIGAFEEE
     LKILLPKEVE SARLELENGN PAIPNRITDR RSYPLYKFVR EELGTVLLTG EKVGSPGEEF
     DKVFTAICAG KLIDPCWSVL KEWNGAPLPL C