ID   PAL2_PETCR              Reviewed;         716 AA.
AC   P45728;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Phenylalanine ammonia-lyase 2;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL2;
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Petroselinum.
OX   NCBI_TaxID=4043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7925471; DOI=10.1111/j.1432-1033.1994.00491.x;
RA   Appert C., Logemann E., Hahlbrock K., Schmid J., Amrhein N.;
RT   "Structural and catalytic properties of the four phenylalanine ammonia-
RT   lyase isoenzymes from parsley (Petroselinum crispum Nym.).";
RL   Eur. J. Biochem. 225:491-499(1994).
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; X81158; CAA57056.1; -; mRNA.
DR   PIR; S48725; S48725.
DR   AlphaFoldDB; P45728; -.
DR   SMR; P45728; -.
DR   KEGG; ag:CAA57056; -.
DR   SABIO-RK; P45728; -.
DR   UniPathway; UPA00713; UER00725.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; TAS:AgBase.
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..716
FT                   /note="Phenylalanine ammonia-lyase 2"
FT                   /id="PRO_0000215407"
FT   ACT_SITE        110
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         384
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         487
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         203
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        202..204
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   716 AA;  77964 MW;  F74D7BD881BEEE66 CRC64;
     MENGNGAITN GHVNGNGMDF CMKTEDPLYW GIAAEAMTGS HLDEVKKMVA EYRKPVVKLG
     GETLTISQVA AISARDGSGV TVELSEAARA GVKASSDWVM DSMNKGTDSY GVTTGFGATS
     HRRTKQGGAL QKELIRFLNA GIFGNGSDNT LPHSATRAAM LVRINTLLQG YSGIRFEILE
     AITKFLNQNI TPCLPLRGTI TASGDLVPLS YIAGLLTGRP NSKAVGPTGV ILSPEEAFKL
     AGVEGGFFEL QPKEGLALVN GTAVGSGMAS MVLFEANILA VLAEVMSAIF AEVMQGKPEF
     TDHLTHKLKH HPGQIEAAAI MEHILDGSAY VKAAQKLHEM DPLQKPKQDR YALRTSPQWL
     GPQIEVIRSS TKMIEREINS VNDNPLIDVS RNKAIHGGNF QGTPIGMSMD NTRLAIAAIG
     KLMFAQFSEL VNDFYNNGLP SNLSGGRNPS LDYGFKGAEI AMASYCSELQ FLANPVTNHV
     QSAEQHNQDV NSLGLISSRK TSEAVEILKL MSTTFLVGLC QAIDLRHLEE NLKSTVKNTV
     SSVAKRVLTM GVNGELHPSR FCEKDLLRFV DREYIFAYID DPCSATYPLM QKLRQTLVEH
     ALKNGDNERN MNTSIFQKIA TFEDELKALL PKEVESARAA LESGNPAIPN RIEECRSYPL
     YKFVRKELGI EYLTGEKVTS PGEEFDKVFI AMSKGEIIDP LLECLESWNG APLPIC