ID   PAL2_LITER              Reviewed;         705 AA.
AC   O49836;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Phenylalanine ammonia-lyase 2;
DE            Short=PAL-2;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
OS   Lithospermum erythrorhizon (Purple gromwell) (Lithospermum officinale var.
OS   erythrorhizon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Boraginales; Boraginaceae; Boraginoideae; Lithospermeae;
OC   Lithospermum.
OX   NCBI_TaxID=34254;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9438980; DOI=10.1271/bbb.61.1995;
RA   Yazaki K., Kataoka M., Honda G., Severin K., Heide L.;
RT   "cDNA cloning and gene expression of phenylalanine ammonia-lyase in
RT   Lithospermum erythrorhizon.";
RL   Biosci. Biotechnol. Biochem. 61:1995-2003(1997).
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   -!- TISSUE SPECIFICITY: Expressed mainly in roots.
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; D83076; BAA24929.1; -; mRNA.
DR   PIR; JC5873; JC5873.
DR   AlphaFoldDB; O49836; -.
DR   SMR; O49836; -.
DR   PRIDE; O49836; -.
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..705
FT                   /note="Phenylalanine ammonia-lyase 2"
FT                   /id="PRO_0000215396"
FT   ACT_SITE        97
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         373
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         476
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         192
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        191..193
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   705 AA;  76510 MW;  ABBEBFF62BC7DB9D CRC64;
     MENGNGKMEF CMKDPLNWGM AAESMKGSHL DEVKKMVAEF RKPVVQLAGK TLTIAQVAAI
     AARDDGVTVE LAEAAREGVK ASSDWVMESM NKGTDSYGVT TGFGATSHRR TKQGGALQKE
     LIRFLNAGIF GNGTETSHTL PHSATRAAML VRINTLLQGY SGIRFEILEA ITKFLNTNIT
     PCLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKAVGPTGEK LNAEEAFRLA GISSGFFELQ
     PKEGLALVNG TAVGSGMASM VLYEANILGV MSEVLSAVFA EVMNGKPEFT DHLTHKLKHH
     PGQIEAAAIM EHILDGSGYV KAAELLHEMD PLQKPKQDRY ALRTSPQWLG PQIEVIRSAT
     KMIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVAMDN TRLAIAAIGK LLFAQFSELV
     NDYYNNGLPS NLTGSRDPSL DYGFKGAEIA MASYCSELQF LANPVTNHVQ SAEQHNQDVN
     SLGLISSRKT SEAVEILKLM SSSFLVALCQ AVDLRHIEEN VRLAVKKTVS QVAKKTLNIG
     VDGVLHPSRF SEKELLRVVD REYVFAYADD PCSATYPLMQ KLREVLVSHA LANSGNEKDA
     STSIFHKIGV FEEELKGILP KEVENARASV ENGTPAIPNK IEECRSYPLY KFVRGELGTE
     LLTGEKVRSP GEELDQVFNA LCEGKLVDPL LACLEAWNGA PLPIC