PAL2_ORYSJ
ID PAL2_ORYSJ Reviewed; 713 AA.
AC Q0DZE0; P53443; Q6K6P7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Phenylalanine ammonia-lyase;
DE EC=4.3.1.24 {ECO:0000250|UniProtKB:P24481};
GN Name=ZB8; OrderedLocusNames=Os02g0627100, LOC_Os02g41680;
GN ORFNames=OsJ_007359, P0042D01.10;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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; AP005000; BAD23155.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09398.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79869.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ23876.1; -; Genomic_DNA.
DR EMBL; AK068993; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015626729.1; XM_015771243.1.
DR AlphaFoldDB; Q0DZE0; -.
DR SMR; Q0DZE0; -.
DR STRING; 4530.OS02T0627100-01; -.
DR PaxDb; Q0DZE0; -.
DR PRIDE; Q0DZE0; -.
DR EnsemblPlants; Os02t0627100-01; Os02t0627100-01; Os02g0627100.
DR GeneID; 4330040; -.
DR Gramene; Os02t0627100-01; Os02t0627100-01; Os02g0627100.
DR KEGG; osa:4330040; -.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_3_0_1; -.
DR InParanoid; Q0DZE0; -.
DR OMA; CNEMIDP; -.
DR OrthoDB; 923557at2759; -.
DR PlantReactome; R-OSA-1119261; Salicylate biosynthesis.
DR PlantReactome; R-OSA-1119418; Suberin biosynthesis.
DR PlantReactome; R-OSA-1119582; Phenylpropanoid biosynthesis, initial reactions.
DR UniPathway; UPA00713; UER00725.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q0DZE0; baseline and differential.
DR Genevisible; Q0DZE0; OS.
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; 1.10.274.20; -; 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 Cytoplasm; Lyase; Phenylalanine catabolism; Phenylpropanoid metabolism;
KW Reference proteome.
FT CHAIN 1..713
FT /note="Phenylalanine ammonia-lyase"
FT /id="PRO_0000215402"
FT ACT_SITE 106
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 484
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 200
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 199..201
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
SQ SEQUENCE 713 AA; 76981 MW; 774C6D2B9B77348A CRC64;
MECENGRVSA NGMSGLCVAA PRADPLNWGK ATEEMTGSHL DEVKRMVAEY RQPLVKIEGA
SLRIAQVAAV AAAGEARVEL DESARERVKA SSDWVMNSMM NGTDSYGVTT GFGATSHRRT
KEGGALQREL IRFLNAGAFG TGTDGHVLPA EATRAAMLVR INTLLQGYSG IRFEILEAIA
KLLNANVTPC LPLRGTITAS GDLVPLSYIA GLVTGRENAV AVAPDGSKVN AAEAFKIAGI
QGGFFELQPK EGLAMVNGTA VGSGLASTVL FEANILAILA EVLSAVFCEV MNGKPEYTDH
LTHKLKHHPG QIEAAAIMEH ILEGSSYMKH AKKLGELDPL MKPKQDRYAL RTSPQWLGPQ
IEVIRAATKS IEREINSVND NPLIDVSRGK ALHGGNFQGT PIGVSMDNTR LAIAAIGKLM
FAQFSELVND FYNNGLPSNL SGGRNPSLDY GFKGAEIAMA SYCSELQFLG NPVTNHVQSA
EQHNQDVNSL GLISSRKTDE AIDILKLMSS TFLIALCQAV DLRHIEENVK SAVKSCVMTV
AKKTLSTNST GDLHVARFCE KDLLKEIDRE AVFAYADDPC SHNYPLMKKL RNVLVERALA
NGAAEFNADT SVFAKVAQFE EELRATLPGA IEAARAAVEN GTAAIPSRIT ECRSYPLYRF
VREELGTKYL TGEKTRSPGE ELNKVLVAIN EGKHIDPLLE CLKEWNGEPL PIC
