PAL1_NARPS
ID PAL1_NARPS Reviewed; 708 AA.
AC A0A2H5AIW0;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Phenylalanine ammonia-lyase 1 {ECO:0000303|PubMed:29229969};
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:Q6GZ04, ECO:0000255|PROSITE-ProRule:PRU10122};
GN Name=PAL1 {ECO:0000303|PubMed:29229969};
OS Narcissus pseudonarcissus (Daffodil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Amaryllidoideae; Narcissus.
OX NCBI_TaxID=39639;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON THE AMARYLLIDACEAE ALKALOID
RP METABOLISM, PATHWAY, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. King Alfred; TISSUE=Bulb;
RX PubMed=29229969; DOI=10.1038/s41598-017-17724-0;
RA Singh A., Desgagne-Penix I.;
RT "Transcriptome and metabolome profiling of Narcissus pseudonarcissus 'King
RT Alfred' reveal components of Amaryllidaceae alkaloid metabolism.";
RL Sci. Rep. 7:17356-17356(2017).
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:Q6GZ04, ECO:0000255|PROSITE-
CC ProRule:PRU10122};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000303|PubMed:29229969}.
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1.
CC {ECO:0000250|UniProtKB:Q6GZ04}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q6GZ04}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11544}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stems, and, to a lower extent,
CC in bulbs, roots, leaves and flowers. {ECO:0000269|PubMed:29229969}.
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; MF405173; AUG71934.1; -; mRNA.
DR AlphaFoldDB; A0A2H5AIW0; -.
DR SMR; A0A2H5AIW0; -.
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:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
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 Alkaloid metabolism; Cytoplasm; Lyase; Phenylalanine catabolism;
KW Phenylpropanoid metabolism.
FT CHAIN 1..708
FT /note="Phenylalanine ammonia-lyase 1"
FT /id="PRO_0000450631"
FT ACT_SITE 100
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 448
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11544"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11544"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 195
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84,
FT ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 194..196
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 708 AA; 76979 MW; E8A8023BA269874C CRC64;
MACANGNGNA NGLCIRDPLS WGAAAEALAG SHLEEVKRMV KEHREACIRL GGATLKVGQI
AAVANGGSAA KVELDESARA RVKASSDWVM DSMSKGTDSY GVTTGFGATS HRRTKQGGAL
QKELIRFLNA GIFGSGRDSC NTLPASTTRA AMLVRINTLL QGYSGIRFEI LEAITRLLNN
NVTPCLPLRG TITASGDLVP LSYIAGILTG RPNSKATAPD GAQIDASEAF RLAGITDGFF
QLQPKEGLAL VNGTAVGSGL ASTVLYDANI LAVLSEVFSA IFCEVMQGKP EFTDHLTHKL
KHHPGQIEAA AVMEHILDGS SYMKMAKKLH ELDPLQKPKQ DRYALRTSPQ WLGPQIEVIR
SATKSIEREI NSVNDNPLID VSRNKALHGG NFQGTPIGVS MDNTRLAIAS IGKLMFAQFS
ELVNDFYNNG LPSNLSGGRD PSLDYGFKGA EIAMASYCSE LQFLANPVTN HVQSAEQHNQ
DVNSLGLISA RKTEEAVHIL KLMSTTFLVG LCQAIDLRHL EENLKSTVKT TISQVAKRVL
TSGINGELHP SRFCEKDLIK VVDREHVFSY VDDPCSATYP LMQRLRQILV EHAMNNGEKE
KDADTSIFRK ISAFEDELKV VLPKEVESAR VAYENGTSAI KNRIEECRSY PLYRFVREET
GTSLLTGENV RSPGEEFDKV FNAICEGRLV DPLLECLEDW NGAPLPIC
