ID PALY_WHEAT Reviewed; 700 AA.
AC Q43210;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Phenylalanine ammonia-lyase;
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN Name=PAL;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RA Liao Y.-C., Li H.-P., Kreuzaler F., Fischer R.;
RT "Nucleotide sequence of one of two tandem genes encoding phenylalanine
RT ammonia-lyase in Triticum aestivum.";
RL (er) Plant Gene Register PGR96-102(1996).
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; X99705; CAA68036.1; -; Genomic_DNA.
DR PIR; T06545; T06545.
DR AlphaFoldDB; Q43210; -.
DR SMR; Q43210; -.
DR STRING; 4565.Q43210; -.
DR PaxDb; 4565-Traes_2AL_9EC3226F7-1; -.
DR eggNOG; KOG0222; Eukaryota.
DR BRENDA; 4.3.1.24; 6500.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q43210; 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; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR01226; phe_am_lyase; 1.
DR PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR PANTHER; PTHR10362:SF81; PHENYLALANINE AMMONIA-LYASE; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 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..700
FT /note="Phenylalanine ammonia-lyase"
FT /id="PRO_0000215428"
FT ACT_SITE 93
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 244
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 332
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 338
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 368
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 440
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:P11544"
FT BINDING 468
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:P11544"
FT BINDING 471
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 187
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 186..188
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 700 AA; 75938 MW; 56EE37B4E74E20B5 CRC64;
MACAWRSRSR ADPLNWGKAA EELSGSHLEA VKRMVEEYRK PVVTMEGATT IAMVAAVAAG
SDTRVELDES ARGRVKESSD WVMNSMMNGT DSYGVTTGFG ATSHRRTKEG GALQRELIRF
LNAGAFGTGT DGHVLPAAAT RAAMLVRVNT LLQGYSGIRF EILETIATLL NANVTPCLPL
RGTITASGDL VPLSYIAGLV TGRPNSMATA PDGSKVNAAE AFKIAGIQHG FFELQPKEGL
AMVNGTAVGS GLASMVLFEA NVLSLLAEVL SGVFCEVMNG KPEFTDHLTH KLKHHPGQIE
AAAIMEHILE GSSYMMLAKK LGELDPLMKP KQDRYALRTS PQWLGPQIEV IRAATKSIER
EINSVNDNPL IDVSRGKAIH GGNFQGTPIG VSMDNTRLAI AAIGKLMFAQ FSELVNDFYN
NGLPSNLSGG RNPSLDYGFK GAEIAMASYC SELQFLGNPV TNHVQSAEQH NQDVNSLGLI
SSRKTAEAID ILKLMSSTFL VALCQAIDLR HLEENVKNAV KSCVKTVARK TLSTDNNGHL
HNARFCEKDL LLTIDREAVF AYADDPCSAN YPLMQKMRAV LVEHALANGE AEAHVETSVF
AKLAMFEQEL RAVLPKEVEA ARSAVENGTA AQQNRIAECR SYPLYRFVRK ELGTEYLTGE
KTRSPGEEVD KVFVAMNQGK HIDALLECLK EWNGEPLPLC
//
