PAL2_NARPS
ID PAL2_NARPS Reviewed; 686 AA.
AC A0A2H5AIY6;
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 2 {ECO:0000303|PubMed:29229969};
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:Q6GZ04, ECO:0000255|PROSITE-ProRule:PRU10122};
GN Name=PAL2 {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 {ECO:0000312|EMBL:AUG71935.1};
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 bulbs, and, to a
CC lower extent, in roots, leaves and flowers.
CC {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; MF405174; AUG71935.1; -; mRNA.
DR AlphaFoldDB; A0A2H5AIY6; -.
DR SMR; A0A2H5AIY6; -.
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..686
FT /note="Phenylalanine ammonia-lyase 2"
FT /id="PRO_0000450632"
FT ACT_SITE 102
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11544"
FT BINDING 478
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11544"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 197
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84,
FT ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 196..198
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 686 AA; 74291 MW; 8108B803C575C70E CRC64;
MEINGNGHVS SPSLCLNKDP LNWGAAAEAL TGSHLDEVKR MVEEYRCSTV RLEGADLKIS
QVAAVAAVAS TVSVELSEAA KDGVKASSEW VRESMAKGTD SYGVTTGFGA TSHRRTKQGG
ALQNELIRFL NAGIFGSGKE SGNTLPASTT RAAMLVRINT LLQGYSGIRF EILEAITALL
NANVTPCLPL RGTITASGDL VPLSYIAGML TGRPNSKAVG PDGTTIDASE AFKLAGIPNG
FFELQPKEGL ALVNGTAVGS GLASTVLFDA NILAVLSEII SAVFCEVMQG KPEFTDHLTH
KLKHHPGQIE AAAIMEHILE GSSYMQMAKK LHELDPLQKP KQDRYALRTS PQWLGPQIEV
IRSSTKSIER EINSVNDNPL IDVSRNKAIH GGNFQGTPIG VSMDNTRLAI AAIGKLMFAQ
ISELVNDFYN NGLPSNLSGG RDPSLDYGFK GAEIAMAAYC SELQYLANPV TNHVQSAEQH
NQDVNSLGLI SSRKTAEAVE ILKLMTSTFL VALCQAIDLR HLEENFKQAV KNTVSQVSKR
VLTTGISGDL HPSRFCEKEL VKVIDREYVF TYIDDPCSYA YPLMQKLRQV LVEHALSNGE
KEKDANTSIF QKIAAFEEEL KAALPKEVEA ARVSVENGSA AIANRIKECR SYPLYRFVRE
ELGARFLTGE KVVSPGEEFD KVFVGI
