ID   PAL2_SOLTU              Reviewed;         590 AA.
AC   P31426;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Phenylalanine ammonia-lyase 2;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
DE   Flags: Fragment;
GN   Name=PAL-2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Datura;
RX   PubMed=1541277; DOI=10.1111/j.1432-1033.1992.tb16675.x;
RA   Joos H.J., Hahlbrock K.;
RT   "Phenylalanine ammonia-lyase in potato (Solanum tuberosum L.). Genomic
RT   complexity, structural comparison of two selected genes and modes of
RT   expression.";
RL   Eur. J. Biochem. 204:621-629(1992).
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; X63104; CAA44818.1; -; Genomic_DNA.
DR   PIR; S70916; S70916.
DR   AlphaFoldDB; P31426; -.
DR   SMR; P31426; -.
DR   InParanoid; P31426; -.
DR   UniPathway; UPA00713; UER00725.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P31426; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
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;
KW   Reference proteome.
FT   CHAIN           1..>590
FT                   /note="Phenylalanine ammonia-lyase 2"
FT                   /id="PRO_0000215420"
FT   ACT_SITE        115
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         494
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         210
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        209..211
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   NON_TER         590
SQ   SEQUENCE   590 AA;  64143 MW;  04B53700FFAE144B CRC64;
     MAPSIAQNEH INGEVKEVLW NLCKKQNYLP LNWEMAADSL RGSKLDQVKK MVDEFRKPIV
     KLGGETLTVA QVASIANVDN KSNGVRVELS ESARAGVKAS SDWVMDSMSK GTDSYGVTTG
     FGATSHRRTK NGGTLQKNLI RFLNAGVFGI GTESTHTLPH SATRAAMLVR INTLLQGYSG
     IRFEILEAIT KLINSNISPC LPLRGTVTAS GDLVPLSYIA GLLTGRPNSK AVGPTGSKLD
     AEEAFRVAGV TGGFFELQPK EGLALVNGTA VGSAMASIVL FESNILAVMF EVLSAIFAEV
     MNGKPEFTDY LTHKLKHHPG QIEAAAIMEH ILDGSSYVKA AQKLHEMDPL QKPKQDRYAL
     RTSPQWLGPQ IEVIRAATKM IEREINSVND NPLIDVSRNK AIHGGNFQGT PIGVSMDNTR
     LALASIGKLM FAQFSELVND YYNNGLPSNL TAGRNPSLDY GFKGAEIAMA SYCSELQFLA
     NPVTNHVQSA EQHNQDVNSL GLISARKTAE AVDILKLMSS TYLVALCQAI DLRHLEENLK
     SVVKNTVSQV AKRTLTIGVL GELHPARFCE KELLRVVDRE YLFAYADDPC