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Protein

Phenylalanine ammonia-lyase 1

Gene

PAL1

Organism
Petroselinum crispum (Parsley) (Petroselinum hortense)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.1 Publication

Catalytic activityi

L-phenylalanine = trans-cinnamate + ammonia.2 Publications

Pathwayi: trans-cinnamate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes trans-cinnamate from L-phenylalanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Phenylalanine ammonia-lyase 3 (PAL3), Phenylalanine ammonia-lyase 2 (PAL2), Phenylalanine ammonia-lyase 1 (PAL1)
This subpathway is part of the pathway trans-cinnamate biosynthesis, which is itself part of Phenylpropanoid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes trans-cinnamate from L-phenylalanine, the pathway trans-cinnamate biosynthesis and in Phenylpropanoid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei110 – 1101Proton donor/acceptorBy similarity
Binding sitei354 – 3541SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Phenylpropanoid metabolism

Enzyme and pathway databases

BRENDAi4.3.1.24. 4694.
SABIO-RKP24481.
UniPathwayiUPA00713; UER00725.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine ammonia-lyase 1 (EC:4.3.1.24)
Gene namesi
Name:PAL1
OrganismiPetroselinum crispum (Parsley) (Petroselinum hortense)
Taxonomic identifieri4043 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeapioid supercladeApieaePetroselinum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi203 – 2031S → A: Complete loss of activity. 1 Publication
Mutagenesisi210 – 2101S → A: No loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 716716Phenylalanine ammonia-lyase 1PRO_0000215406Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki202 ↔ 2045-imidazolinone (Ala-Gly)
Modified residuei203 – 20312,3-didehydroalanine (Ser)

Post-translational modificationi

Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.

Proteomic databases

PRIDEiP24481.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1
716
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 356Combined sources
Helixi41 – 5212Combined sources
Beta strandi55 – 595Combined sources
Helixi66 – 738Combined sources
Beta strandi81 – 844Combined sources
Helixi86 – 883Combined sources
Helixi89 – 10315Combined sources
Turni105 – 1084Combined sources
Beta strandi122 – 1265Combined sources
Helixi129 – 13810Combined sources
Beta strandi145 – 1473Combined sources
Helixi153 – 16513Combined sources
Turni166 – 1694Combined sources
Helixi176 – 18712Combined sources
Beta strandi195 – 1973Combined sources
Beta strandi201 – 2044Combined sources
Helixi206 – 21611Combined sources
Helixi234 – 2418Combined sources
Beta strandi244 – 2463Combined sources
Helixi254 – 2596Combined sources
Helixi263 – 29432Combined sources
Helixi298 – 3014Combined sources
Helixi303 – 3075Combined sources
Helixi312 – 32615Combined sources
Beta strandi345 – 3473Combined sources
Helixi351 – 3544Combined sources
Helixi356 – 37722Combined sources
Beta strandi384 – 3885Combined sources
Turni389 – 3924Combined sources
Beta strandi393 – 3953Combined sources
Helixi403 – 43028Combined sources
Turni433 – 4353Combined sources
Helixi441 – 4433Combined sources
Helixi449 – 4513Combined sources
Helixi456 – 47217Combined sources
Turni484 – 4874Combined sources
Beta strandi488 – 4903Combined sources
Helixi494 – 54754Combined sources
Turni551 – 5533Combined sources
Helixi560 – 57213Combined sources
Helixi575 – 5773Combined sources
Turni578 – 5803Combined sources
Helixi588 – 60215Combined sources
Helixi605 – 6095Combined sources
Helixi611 – 6133Combined sources
Helixi616 – 6183Combined sources
Helixi619 – 64224Combined sources
Helixi651 – 6544Combined sources
Helixi658 – 6658Combined sources
Helixi681 – 69313Combined sources
Turni694 – 6974Combined sources
Helixi698 – 7036Combined sources
Turni704 – 7074Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W27X-ray1.70A/B1-716[»]
ProteinModelPortaliP24481.
SMRiP24481. Positions 25-716.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24481.

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Phylogenomic databases

KOiK10775.

Family and domain databases

Gene3Di1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProiIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
IPR005922. Phe_NH3-lyase.
IPR023144. Phe_NH3-lyase_shielding_dom.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01226. phe_am_lyase. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24481-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENGNGATTN GHVNGNGMDF CMKTEDPLYW GIAAEAMTGS HLDEVKKMVA
60 70 80 90 100
EYRKPVVKLG GETLTISQVA AISARDGSGV TVELSEAARA GVKASSDWVM
110 120 130 140 150
DSMNKGTDSY GVTTGFGATS HRRTKQGGAL QKELIRFLNA GIFGNGSDNT
160 170 180 190 200
LPHSATRAAM LVRINTLLQG YSGIRFEILE AITKFLNQNI TPCLPLRGTI
210 220 230 240 250
TASGDLVPLS YIAGLLTGRP NSKAVGPTGV ILSPEEAFKL AGVEGGFFEL
260 270 280 290 300
QPKEGLALVN GTAVGSGMAS MVLFEANILA VLAEVMSAIF AEVMQGKPEF
310 320 330 340 350
TDHLTHKLKH HPGQIEAAAI MEHILDGSAY VKAAQKLHEM DPLQKPKQDR
360 370 380 390 400
YALRTSPQWL GPQIEVIRSS TKMIEREINS VNDNPLIDVS RNKAIHGGNF
410 420 430 440 450
QGTPIGVSMD NTRLAIAAIG KLMFAQFSEL VNDFYNNGLP SNLSGGRNPS
460 470 480 490 500
LDYGFKGAEI AMASYCSELQ FLANPVTNHV QSAEQHNQDV NSLGLISSRK
510 520 530 540 550
TSEAVEILKL MSTTFLVGLC QAIDLRHLEE NLKSTVKNTV SSVAKRVLTM
560 570 580 590 600
GVNGELHPSR FCEKDLLRVV DREYIFAYID DPCSATYPLM QKLRQTLVEH
610 620 630 640 650
ALKNGDNERN LSTSIFQKIA TFEDELKALL PKEVESARAA LESGNPAIPN
660 670 680 690 700
RIEECRSYPL YKFVRKELGT EYLTGEKVTS PGEEFEKVFI AMSKGEIIDP
710
LLECLESWNG APLPIC
Length:716
Mass (Da):77,829
Last modified:March 1, 1992 - v1
Checksum:i23D82FA1AC6FBB4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15473 Genomic DNA. Translation: CAA33500.1.
X16772 Genomic DNA. Translation: CAA34715.1.
Y07654 Genomic DNA. Translation: CAA68938.1.
PIRiS04463.

Genome annotation databases

KEGGiag:CAA68938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15473 Genomic DNA. Translation: CAA33500.1.
X16772 Genomic DNA. Translation: CAA34715.1.
Y07654 Genomic DNA. Translation: CAA68938.1.
PIRiS04463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W27X-ray1.70A/B1-716[»]
ProteinModelPortaliP24481.
SMRiP24481. Positions 25-716.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP24481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA68938.

Phylogenomic databases

KOiK10775.

Enzyme and pathway databases

UniPathwayiUPA00713; UER00725.
BRENDAi4.3.1.24. 4694.
SABIO-RKP24481.

Miscellaneous databases

EvolutionaryTraceiP24481.

Family and domain databases

Gene3Di1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProiIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
IPR005922. Phe_NH3-lyase.
IPR023144. Phe_NH3-lyase_shielding_dom.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01226. phe_am_lyase. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A phenylalanine ammonia-lyase gene from parsley: structure, regulation and identification of elicitor and light responsive cis-acting elements."
    Lois R., Dietrich A., Hahlbrock K., Schulz W.
    EMBO J. 8:1641-1648(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Kang X., Logemann E., Hahlbrock K.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Serine-202 is the putative precursor of the active site dehydroalanine of phenylalanine ammonia lyase. Site-directed mutagenesis studies on the enzyme from parsley (Petroselinum crispum L.)."
    Schuster B., Retey J.
    FEBS Lett. 349:252-254(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME MECHANISM, DEHYDROALANINE FORMATION, MUTAGENESIS OF SER-203 AND SER-210.
  4. "Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase."
    Ritter H., Schulz G.E.
    Plant Cell 16:3426-3436(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PTM.

Entry informationi

Entry nameiPAL1_PETCR
AccessioniPrimary (citable) accession number: P24481
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 8, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.