ID   PAL3_PETCR              Reviewed;         718 AA.
AC   P45729;
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 3;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL3;
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; X81159; CAA57057.1; -; mRNA.
DR   PIR; S48726; S48726.
DR   AlphaFoldDB; P45729; -.
DR   SMR; P45729; -.
DR   KEGG; ag:CAA57057; -.
DR   SABIO-RK; P45729; -.
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..718
FT                   /note="Phenylalanine ammonia-lyase 3"
FT                   /id="PRO_0000215408"
FT   ACT_SITE        109
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         350
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         386
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         489
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         205
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        204..206
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   718 AA;  78165 MW;  17786451FFDBDC35 CRC64;
     MAYVNGTTNG HANGNGLDLC MKKEDPLNWG VAAEALTGSH LDEVKRMVAE YRKPVVKLEG
     ETLTISQVAA ISARDDSGVK VELSEEARAG VKASSDWVMD SMNKGTDSYG VTTGFGATSH
     RRTKQGGALQ KELIRFLNAG IFGSGAEAGN NTLPHSATRA AMLVRINTLL QGYSGIRFEI
     LEAITKFLNH NITPCLPLRG TITASGDLVP LSYIAGLLTG RPNSKAVGPT GVTLSPEEAF
     KLAGVEGGFF ELQPKEGLAL VNGTAVGSGM ASMVLFEANI LAVLAEVMSA IFAEVMQGKP
     EFTDHLTHKL KHHPGQIEAA AIMEHILDGS AYVKAAQKLH EMDPLQKPKQ DRYALRTSPQ
     WLGPQIEVIR SSTKMIEREI NSVNDNPLID VSRNKAIHGG NFQGSPIGVS MDNTRLAIAA
     IGKLMFAQFS ELVNDFYNNG LPSNLSGGRN PSLDYGFKGA EIAMASYCSE LQFLANPVTN
     HVQSAEQHNQ DVNSLGLISS RKTSEAVEIL KLMSTTFLVG LCQAIDLRHL EENLKSTVKN
     TVSQVAKRVL TMGVNGELHP SRFCEKDLLR VVDREYIFAY IDDPCSATYP LMQKLRETLV
     EHALNNGDKE RNLSTSIFQK IAAFEDELKA LLPKEVETAR AALESGNPAI PNRIKECRSY
     PLYKFVREEL GTEYLTGEKV RSPGEEFEKV FTAMSKGEII DPLLECLESW NGAPLPIC