PAL1_PETCR
ID PAL1_PETCR Reviewed; 716 AA.
AC P24481;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phenylalanine ammonia-lyase 1 {ECO:0000303|PubMed:2767049};
DE EC=4.3.1.24 {ECO:0000269|PubMed:15548745, ECO:0000269|PubMed:8050576};
GN Name=PAL1;
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2767049; DOI=10.1002/j.1460-2075.1989.tb03554.x;
RA Lois R., Dietrich A., Hahlbrock K., Schulz W.;
RT "A phenylalanine ammonia-lyase gene from parsley: structure, regulation and
RT identification of elicitor and light responsive cis-acting elements.";
RL EMBO J. 8:1641-1648(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kang X., Logemann E., Hahlbrock K.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CATALYTIC ACTIVITY, ENZYME MECHANISM, DEHYDRATION AT SER-203, AND
RP MUTAGENESIS OF SER-203 AND SER-210.
RX PubMed=8050576; DOI=10.1016/0014-5793(94)00681-4;
RA Schuster B., Retey J.;
RT "Serine-202 is the putative precursor of the active site dehydroalanine of
RT phenylalanine ammonia lyase. Site-directed mutagenesis studies on the
RT enzyme from parsley (Petroselinum crispum L.).";
RL FEBS Lett. 349:252-254(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND PTM.
RX PubMed=15548745; DOI=10.1105/tpc.104.025288;
RA Ritter H., Schulz G.E.;
RT "Structural basis for the entrance into the phenylpropanoid metabolism
RT catalyzed by phenylalanine ammonia-lyase.";
RL Plant Cell 16:3426-3436(2004).
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:15548745}.
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:15548745, ECO:0000269|PubMed:8050576};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-cinnamate biosynthesis;
CC trans-cinnamate from L-phenylalanine: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15548745}.
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; X15473; CAA33500.1; -; Genomic_DNA.
DR EMBL; X16772; CAA34715.1; -; Genomic_DNA.
DR EMBL; Y07654; CAA68938.1; -; Genomic_DNA.
DR PIR; S04463; S04463.
DR PDB; 1W27; X-ray; 1.70 A; A/B=1-716.
DR PDB; 6F6T; X-ray; 1.90 A; A/B=1-716.
DR PDB; 6H2O; X-ray; 1.90 A; A/B=1-716.
DR PDB; 6HQF; X-ray; 1.76 A; A/B=1-716.
DR PDB; 6RGS; X-ray; 2.42 A; A/B=1-715.
DR PDBsum; 1W27; -.
DR PDBsum; 6F6T; -.
DR PDBsum; 6H2O; -.
DR PDBsum; 6HQF; -.
DR PDBsum; 6RGS; -.
DR AlphaFoldDB; P24481; -.
DR SMR; P24481; -.
DR KEGG; ag:CAA68938; -.
DR BRENDA; 4.3.1.24; 4694.
DR SABIO-RK; P24481; -.
DR UniPathway; UPA00713; UER00725.
DR EvolutionaryTrace; P24481; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; TAS:AgBase.
DR GO; GO:0016597; F:amino acid binding; TAS:AgBase.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lyase; Phenylalanine catabolism;
KW Phenylpropanoid metabolism.
FT CHAIN 1..716
FT /note="Phenylalanine ammonia-lyase 1"
FT /id="PRO_0000215406"
FT ACT_SITE 110
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 354
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT BINDING 487
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MOD_RES 203
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:8050576"
FT CROSSLNK 202..204
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250|UniProtKB:Q68G84"
FT MUTAGEN 203
FT /note="S->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:8050576"
FT MUTAGEN 210
FT /note="S->A: No loss of activity."
FT /evidence="ECO:0000269|PubMed:8050576"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:1W27"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:1W27"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6HQF"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6HQF"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:1W27"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:1W27"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 234..241
FT /evidence="ECO:0007829|PDB:1W27"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 263..294
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:6HQF"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 356..377
FT /evidence="ECO:0007829|PDB:1W27"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 389..392
FT /evidence="ECO:0007829|PDB:1W27"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 403..430
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 456..472
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 484..487
FT /evidence="ECO:0007829|PDB:1W27"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 494..547
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 551..553
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 560..572
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 588..602
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 605..609
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 619..642
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 651..654
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 658..665
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:6RGS"
FT HELIX 681..693
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 694..697
FT /evidence="ECO:0007829|PDB:1W27"
FT HELIX 698..703
FT /evidence="ECO:0007829|PDB:1W27"
FT TURN 704..707
FT /evidence="ECO:0007829|PDB:1W27"
SQ SEQUENCE 716 AA; 77829 MW; 23D82FA1AC6FBB4A CRC64;
MENGNGATTN GHVNGNGMDF CMKTEDPLYW GIAAEAMTGS HLDEVKKMVA EYRKPVVKLG
GETLTISQVA AISARDGSGV TVELSEAARA GVKASSDWVM DSMNKGTDSY GVTTGFGATS
HRRTKQGGAL QKELIRFLNA GIFGNGSDNT LPHSATRAAM LVRINTLLQG YSGIRFEILE
AITKFLNQNI TPCLPLRGTI TASGDLVPLS YIAGLLTGRP NSKAVGPTGV ILSPEEAFKL
AGVEGGFFEL QPKEGLALVN GTAVGSGMAS MVLFEANILA VLAEVMSAIF AEVMQGKPEF
TDHLTHKLKH HPGQIEAAAI MEHILDGSAY VKAAQKLHEM DPLQKPKQDR YALRTSPQWL
GPQIEVIRSS TKMIEREINS VNDNPLIDVS RNKAIHGGNF QGTPIGVSMD NTRLAIAAIG
KLMFAQFSEL VNDFYNNGLP SNLSGGRNPS LDYGFKGAEI AMASYCSELQ FLANPVTNHV
QSAEQHNQDV NSLGLISSRK TSEAVEILKL MSTTFLVGLC QAIDLRHLEE NLKSTVKNTV
SSVAKRVLTM GVNGELHPSR FCEKDLLRVV DREYIFAYID DPCSATYPLM QKLRQTLVEH
ALKNGDNERN LSTSIFQKIA TFEDELKALL PKEVESARAA LESGNPAIPN RIEECRSYPL
YKFVRKELGT EYLTGEKVTS PGEEFEKVFI AMSKGEIIDP LLECLESWNG APLPIC
