PAL1_PETHY
ID PAL1_PETHY Reviewed; 718 AA.
AC Q50EX7;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Phenylalanine ammonia-lyase 1 {ECO:0000303|PubMed:15805488};
DE Short=PhPAL1 {ECO:0000303|PubMed:15805488};
DE EC=4.3.1.24 {ECO:0000269|PubMed:20070567};
GN Name=PAL1 {ECO:0000303|PubMed:15805488};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Mitchell;
RX PubMed=15805488; DOI=10.1105/tpc.104.028837;
RA Verdonk J.C., Haring M.A., van Tunen A.J., Schuurink R.C.;
RT "ODORANT1 regulates fragrance biosynthesis in petunia flowers.";
RL Plant Cell 17:1612-1624(2005).
RN [2]
RP INDUCTION.
RC STRAIN=cv. W115;
RX PubMed=12590126; DOI=10.1016/s0031-9422(02)00707-0;
RA Verdonk J.C., Ric de Vos C.H., Verhoeven H.A., Haring M.A., van Tunen A.J.,
RA Schuurink R.C.;
RT "Regulation of floral scent production in petunia revealed by targeted
RT metabolomics.";
RL Phytochemistry 62:997-1008(2003).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=20070567; DOI=10.1111/j.1365-313x.2010.04127.x;
RA Colon A.M., Sengupta N., Rhodes D., Dudareva N., Morgan J.;
RT "A kinetic model describes metabolic response to perturbations and
RT distribution of flux control in the benzenoid network of Petunia hybrida.";
RL Plant J. 62:64-76(2010).
RN [4]
RP INDUCTION BY EOBI.
RC STRAIN=cv. W115;
RX PubMed=23275577; DOI=10.1105/tpc.112.105247;
RA Spitzer-Rimon B., Farhi M., Albo B., Cna'ani A., Ben Zvi M.M., Masci T.,
RA Edelbaum O., Yu Y., Shklarman E., Ovadis M., Vainstein A.;
RT "The R2R3-MYB-like regulatory factor EOBI, acting downstream of EOBII,
RT regulates scent production by activating ODO1 and structural scent-related
RT genes in petunia.";
RL Plant Cell 24:5089-5105(2012).
RN [5]
RP INDUCTION.
RX PubMed=26124104; DOI=10.1073/pnas.1422875112;
RA Fenske M.P., Hewett Hazelton K.D., Hempton A.K., Shim J.S., Yamamoto B.M.,
RA Riffell J.A., Imaizumi T.;
RT "Circadian clock gene LATE ELONGATED HYPOCOTYL directly regulates the
RT timing of floral scent emission in Petunia.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:9775-9780(2015).
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:0000269|PubMed:20070567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21385;
CC Evidence={ECO:0000269|PubMed:20070567};
CC -!- ACTIVITY REGULATION: Competitive inhibition by cinnamic acid (CA).
CC {ECO:0000269|PubMed:20070567}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=160 uM for L-phenylalanine {ECO:0000269|PubMed:20070567};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1.
CC {ECO:0000250|UniProtKB:P24481}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P24481}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P24481}.
CC -!- INDUCTION: Circadian-regulation with peak levels occurring at the end
CC of the light period in flowers (PubMed:26124104, PubMed:12590126).
CC Triggered by EOBI in flowers via the regulation of its promoter
CC (PubMed:23275577). {ECO:0000269|PubMed:12590126,
CC ECO:0000269|PubMed:23275577, ECO:0000269|PubMed:26124104}.
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; AY705976; AAV98199.1; -; mRNA.
DR AlphaFoldDB; Q50EX7; -.
DR SMR; Q50EX7; -.
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:0007623; P:circadian rhythm; IEP:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism.
FT CHAIN 1..718
FT /note="Phenylalanine ammonia-lyase 1"
FT /id="PRO_0000451488"
FT ACT_SITE 110
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 205
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT CROSSLNK 204..206
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 718 AA; 78601 MW; CD8B83FFF50AE09F CRC64;
MEYANENCNG HASQDICVKG HDQQLDPLNW NMAADALKGS HLDEVKRMVK EFRKPVVRLG
GETLTVAQVA AIASQSGTDV TVQLSEASRA GVKASSDWVL QGMINGTDSY GVTTGFGATS
HRRTKEGAAL QKELIRFLNA GIFGNGTESS HTLPHSATRA AMLVRINTLL QGYSGIRFEI
LEAITKLLNN NITPCLPLRG TITASGDLVP LSYIAGLLTG RPNSKATGPN GELLDAVKAF
QRAGIDTGFF ELQPKEGLAL VNGTAVGSGL ASMVLFDANI LAVLSEVLSA IFAEVMQGKP
EFTDYLTHKL KHHPGQIEAA AIMEHILDGS SYVKEAKIVH EMDPLQKPKQ DRYALRTSPQ
WLGPQIEVIR AATKMIEREI NSVNDNPLID VSRNKALHGG NFQGTPIGVS MDNTRLALAS
IGKLMFAQFS ELVNDYYNNG LPSNLTGGRN PSLDYGFKGA EIAMASYCSE LQFLANPVTN
HVQSAEQHNQ DVNSLGLISS RKTAEAVDIL KLMSSTYLVA LCQAIDLRHL EENLKATVKN
SVSLVAKKVL TIGEKGELHH SRFCEKDMLK VVDREYIFAY ADDACSATYP LMQKLRQVLV
DRALLNVDGE KDSSTSIFQK IKAFEEELKV VLPKEIERAR SDLEQGKPAI PNRIQECRSY
PLYKFVREEL KANYLTGEKV QSPGEEFDKV FTAMNEGKLV DPLLNCLKEW NGAPLPLC
