PAL1_ARATH
ID PAL1_ARATH Reviewed; 725 AA.
AC P35510; Q94AN1; Q9ZQD6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Phenylalanine ammonia-lyase 1;
DE EC=4.3.1.24 {ECO:0000269|PubMed:15276452};
GN Name=PAL1; OrderedLocusNames=At2g37040; ORFNames=T1J8.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7888622; DOI=10.1007/bf00020187;
RA Wanner L.A., Li G., Ware D., Somssich I.E., Davis K.R.;
RT "The phenylalanine ammonia-lyase gene family in Arabidopsis thaliana.";
RL Plant Mol. Biol. 27:327-338(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=15276452; DOI=10.1016/j.phytochem.2004.05.006;
RA Cochrane F.C., Davin L.B., Lewis N.G.;
RT "The Arabidopsis phenylalanine ammonia lyase gene family: kinetic
RT characterization of the four PAL isoforms.";
RL Phytochemistry 65:1557-1564(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-240.
RC STRAIN=cv. Columbia;
RX PubMed=2152131; DOI=10.2307/3869320;
RA Ohl S., Hedrick S.A., Chory J., Lamb C.J.;
RT "Functional properties of a phenylalanine ammonia-lyase promoter from
RT Arabidopsis.";
RL Plant Cell 2:837-848(1990).
RN [7]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
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:0000269|PubMed:15276452}.
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:15276452};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=68 uM for L-phenylalanine {ECO:0000269|PubMed:15276452};
CC Vmax=5.5 umol/sec/mg enzyme {ECO:0000269|PubMed:15276452};
CC pH dependence:
CC Optimum pH is 8.4-9.2. {ECO:0000269|PubMed:15276452};
CC Temperature dependence:
CC Optimum temperature is 46-48 degrees Celsius.
CC {ECO:0000269|PubMed:15276452};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L33677; AAC18870.1; -; Genomic_DNA.
DR EMBL; AY303128; AAP59438.1; -; mRNA.
DR EMBL; AC006922; AAM15324.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09341.1; -; Genomic_DNA.
DR EMBL; AY045919; AAK76593.1; -; mRNA.
DR EMBL; AY079363; AAL85094.1; -; mRNA.
DR EMBL; BT003330; AAO29949.1; -; mRNA.
DR EMBL; X62747; CAA44609.1; -; Genomic_DNA.
DR PIR; G84787; G84787.
DR PIR; S52990; S52990.
DR RefSeq; NP_181241.1; NM_129260.3.
DR AlphaFoldDB; P35510; -.
DR SMR; P35510; -.
DR BioGRID; 3624; 9.
DR IntAct; P35510; 4.
DR STRING; 3702.AT2G37040.1; -.
DR iPTMnet; P35510; -.
DR PaxDb; P35510; -.
DR PRIDE; P35510; -.
DR ProteomicsDB; 248746; -.
DR EnsemblPlants; AT2G37040.1; AT2G37040.1; AT2G37040.
DR GeneID; 818280; -.
DR Gramene; AT2G37040.1; AT2G37040.1; AT2G37040.
DR KEGG; ath:AT2G37040; -.
DR Araport; AT2G37040; -.
DR TAIR; locus:2057981; AT2G37040.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_3_0_1; -.
DR InParanoid; P35510; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 923557at2759; -.
DR PhylomeDB; P35510; -.
DR BRENDA; 4.3.1.24; 399.
DR SABIO-RK; P35510; -.
DR UniPathway; UPA00713; UER00725.
DR PRO; PR:P35510; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P35510; baseline and differential.
DR Genevisible; P35510; AT.
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; IDA:TAIR.
DR GO; GO:0009800; P:cinnamic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006952; P:defense response; IEP:TAIR.
DR GO; GO:0009819; P:drought recovery; IMP:TAIR.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046274; P:lignin catabolic process; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR GO; GO:0046244; P:salicylic acid catabolic process; IMP:TAIR.
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;
KW Reference proteome.
FT CHAIN 1..725
FT /note="Phenylalanine ammonia-lyase 1"
FT /id="PRO_0000215382"
FT ACT_SITE 117
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 496
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 212
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 211..213
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT CONFLICT 329
FT /note="I -> V (in Ref. 1; AAC18870)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="A -> R (in Ref. 1; AAC18870)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="I -> V (in Ref. 1; AAC18870)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 78726 MW; 02626B3B2DEFE9CE CRC64;
MEINGAHKSN GGGVDAMLCG GDIKTKNMVI NAEDPLNWGA AAEQMKGSHL DEVKRMVAEF
RKPVVNLGGE TLTIGQVAAI STIGNSVKVE LSETARAGVN ASSDWVMESM NKGTDSYGVT
TGFGATSHRR TKNGVALQKE LIRFLNAGIF GSTKETSHTL PHSATRAAML VRINTLLQGF
SGIRFEILEA ITSFLNNNIT PSLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKATGPNGEA
LTAEEAFKLA GISSGFFDLQ PKEGLALVNG TAVGSGMASM VLFETNVLSV LAEILSAVFA
EVMSGKPEFT DHLTHRLKHH PGQIEAAAIM EHILDGSSYM KLAQKLHEMD PLQKPKQDRY
ALRTSPQWLG PQIEVIRYAT KSIEREINSV NDNPLIDVSR NKAIHGGNFQ GTPIGVSMDN
TRLAIAAIGK LMFAQFSELV NDFYNNGLPS NLTASRNPSL DYGFKGAEIA MASYCSELQY
LANPVTSHVQ SAEQHNQDVN SLGLISSRKT SEAVDILKLM STTFLVAICQ AVDLRHLEEN
LRQTVKNTVS QVAKKVLTTG VNGELHPSRF CEKDLLKVVD REQVYTYADD PCSATYPLIQ
KLRQVIVDHA LINGESEKNA VTSIFHKIGA FEEELKAVLP KEVEAARAAY DNGTSAIPNR
IKECRSYPLY RFVREELGTE LLTGEKVTSP GEEFDKVFTA ICEGKIIDPM MECLNEWNGA
PIPIC
