ID   PALY_STYHU              Reviewed;         715 AA.
AC   P45732;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Phenylalanine ammonia-lyase;
DE            EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN   Name=PAL17.1;
OS   Stylosanthes humilis (Townsville stylo) (Astyposanthes humilis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Stylosanthes.
OX   NCBI_TaxID=35628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Paterson; TISSUE=Stem;
RX   PubMed=7630950; DOI=10.1104/pp.108.3.1301;
RA   Manners J.M., McIntyre C.L., Nourse J.P.;
RT   "Cloning and sequence of a cDNA encoding phenylalanine ammonia-lyase from
RT   the tropical forage legume Stylosanthes humilis.";
RL   Plant Physiol. 108:1301-1302(1995).
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; L36822; AAA99500.1; -; mRNA.
DR   AlphaFoldDB; P45732; -.
DR   SMR; P45732; -.
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..715
FT                   /note="Phenylalanine ammonia-lyase"
FT                   /id="PRO_0000215422"
FT   ACT_SITE        107
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   BINDING         486
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
FT   MOD_RES         202
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   CROSSLNK        201..203
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ   SEQUENCE   715 AA;  77954 MW;  8D81EC3D5E4F6A2D CRC64;
     MDTHANADAT FCLTANNGQQ PRHDPLNWAA AAEALKGSHL DEVKRMVSEY RKPLVNLGGQ
     TLTISQVAAI AANDQGVSVQ LSEASRAGVK ASSDWVMDSM NNGTDSYGVT TGFGATSHRR
     TKQGGALQKE LIRFLNAGIF GNGTETNCTL PHTATRAAML VRINTLLQGY SGIRFEILEA
     ITKLLNNNIT PCLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKAVGPNGET LNAKEAFQAA
     GIGSDFFELQ PKEGLALVNG TPVGSGLASV VLFEANILAV LSEVLSAIFA EVMQGKPEFT
     DHLTHKLKHH PGQIEAAAIM EHILDGSSYV KAAKKLHEID PLQKPKQDRY ALRTSPQWLG
     PLVEVIRFST KSIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVSMDN TRLAVASIGK
     LMFAQFSELV NDFYNNGLPS NLSASRNPSL DYGFKGTEIA MASYCSELQY LANPVTSHVQ
     SAEQHNQDVN SLGLISARKT NEAVEILKLM SPTYLIALCQ AIDLRHLEEN LKNTVKNTVS
     QVAKRTLTTG VNGELHPSRF CEKDLLKIVD REYCFAYIDD PCSATYPLMQ KLRQVLVEHA
     LANAENEKNV NTSIFQKITT FEEELKTLLP KEVEGARIAY ENGQSAIPNK IKECRSYPLY
     KFVREELGTE MLTGEKVRSP GEECDKLFTA MCQGKIIDPL LECIGEWNGA PLPLC