ID   PALY_CITLI              Reviewed;         722 AA.
AC   Q42667;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL6;
OS   Citrus limon (Lemon) (Citrus medica var. limon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seelenfreund D., Chiong M., Lobos S., Perez L.M.;
RT   "A full-length cDNA coding for phenylalanine ammonia-lyase from Citrus
RT   limon.";
RL   (er) Plant Gene Register PGR96-026(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; U43338; AAB67733.1; -; mRNA.
DR   AlphaFoldDB; Q42667; -.
DR   SMR; Q42667; -.
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..722
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215389"
FT   ACT_SITE        112
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         491
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         207
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        206..208
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   722 AA;  78490 MW;  C96893196E30D9E5 CRC64;
     MELSHETCNG IKNDRNGGTS SLGLCTGTDP LNWTVAADSL KGSHLDEVKR MIDEYRRPVV
     KLGGESLTIG QVTAIAAHDS GVKVELAEAA RAGVKASSDW VMDSMMKGTD SYGVTTGFGA
     TSHRRTKQGG ALQKELIRFL NSGIFGNGTE SSHTLPHSAT RAAMLVRVNT LLQGYSGIRF
     EILETITKFL NHNITPCLPL RGTITASGDL VPLSYIAGLL TGRPNSKAVG SNGQVLNPTE
     AFNLAGVTSG FFELQPKEGL ALVNGTAVGS GLAATVLFEA NILAIMSEVL SAIFAEVMNG
     KPEFTDHLTH KLKHHPGQIE AAAIMEHILD GSSYVKAAQK LHETDPLQKP KQDRYALRTS
     PQWLGPQIEV IRAATKMIER EINSVNDNPL IDVSRNKALH GGNFQGTPIG VSMDNTRLAI
     ASIGKLMFAQ FSELVNDFYN NGLPSNLTGG RNPSLDYGFK GAEIAMASYC SELQFLANPV
     TNHVQSAEQH NQDVNSLGLN SSRKTAEAVD ILKLMSSTFL VALCQAIDLR HLEENLKNTV
     KNTVSQVAKR VLTMGVNGEL HPSRFCEKDL IKVVDREYVF AYIDDPCSAS SPLMQKLRQV
     LVDHALDNGD REKNSTTSIF QKIGAFEDEL KTLLPKEVEI ARTELESGNA AIPNRIKECR
     SYPLYKIVRE DIGTSLLTGE KVRSPGEEFD KVFTAMCEGK LIDPMLECLK EWNGAPLPIC
     QN