Q9M568 (PAL1_RUBID) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenylalanine ammonia-lyase 1
EC=4.3.1.24

Alternative name(s):
RiPAL1

Gene names

Name:

PAL1

Organism

Rubus idaeus (Raspberry)

Taxonomic identifier

32247 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Rosaceae › Rosoideae › Rosodae › Rubus

Protein attributes

Sequence length	710 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Catalytic activity	L-phenylalanine = trans-cinnamate + ammonia.
Pathway	Phenylpropanoid metabolism; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1.
Subcellular location	Cytoplasm Probable.
Developmental stage	Early fruit ripening.
Post-translational modification	Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly By similarity.
Sequence similarities	Belongs to the PAL/histidase family.

Ontologies

Keywords
Biological process	Phenylpropanoid metabolism
Cellular component	Cytoplasm
Molecular function	Lyase
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: InterPro biosynthetic process Inferred from electronic annotation. Source: InterPro phenylpropanoid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ammonia-lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 710	710	Phenylalanine ammonia-lyase 1		PRO_0000215418
Amino acid modifications
	Modified residue	197	1	2,3-didehydroalanine (Ser) By similarity
	Cross-link	196 ↔ 198		5-imidazolinone (Ala-Gly) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9M568 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 8ED569D63C0D5167	FASTA	710	77,746
	10 20 30 40 50 60 MEFYKNGNGA VESFCEGHDP LNWNMAAESL KGSHVDELKR MVSDYRKPVV KLGGETLTIG 70 80 90 100 110 120 QVAAIASHDG GVRVELSEEK RAGVKASSDW VMDSMGKGTD SYGVTTGFGA TSHRRTKNGG 130 140 150 160 170 180 ALQRELIRFL NAGIFGSSLD STHKLPHTAT RAAMLVRFNT LLQGYSGIRF EILEAITKFL 190 200 210 220 230 240 NGNITPCLPL RGTITASGDL VPLSYIAGLL IGRPNSKSVG PKGETLSPAE GFKLAGIDGG 250 260 270 280 290 300 FFELQPKEGL ALVNGTAVGS GMASMVLFDA NTLAVLSEVM SAIFAEVMQG KPEFTDHLTH 310 320 330 340 350 360 KLKHHPGQIE AAAIMEHILE GSSYVKEAKK VHEMDPLQKP KQDRYALRTS PQWLGPQIEV 370 380 390 400 410 420 IRAATKMIER EINSVNDNPL IDVSRNKALH GGNFQELPIG VAMDNTRLAI ASIGKLIFAQ 430 440 450 460 470 480 FSELVNDYYN NGLPSILTGS SNPSLDYGFK GAEIAMASYC SELQFLANPV TNHVQSAEQH 490 500 510 520 530 540 NQDVNSLGLI SSRKTSEAVD ILKLMSSTFL VALCQAIDLR HLEENLKIVV KTTVSNVAKR 550 560 570 580 590 600 TLTVSPNGEL HPSRFSEKDL LTVVDREYLF SYIDDPCLAT YPLMQKLRAE LVEHALKNGE 610 620 630 640 650 660 RERSANTSIF HKIAAFEEEL KTILPKEVDN ARIEIENGKS EIPNRIKECR SYPLYRFVRE 670 680 690 700 710 ELGTSLLTGE KIKSPGEECY KVFNAICAGK LVDPLLECLK EWNGAPLPIS

References

[1]	"The phenylalanine ammonia-lyase gene family in raspberry. Structure, expression, and evolution." Kumar A., Ellis B.E. Plant Physiol. 127:230-239(2001) [PubMed: 11553751] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fruit.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF237954 mRNA. Translation: AAF40223.1.
3D structure databases
ProteinModelPortal	Q9M568.
SMR	Q9M568. Positions 19-709.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR001106. Phe/His_NH3-lyase. IPR022313. Phe/His_NH3-lyase_AS. IPR005922. Phe_NH3-lyase. IPR023144. Phe_NH3-lyase_shielding_dom. [Graphical view]
Gene3D	G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit. G3DSA:1.10.274.20. Phe_NH3-lyase_shielding_dom. 1 hit.
Pfam	PF00221. PAL. 1 hit. [Graphical view]
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR01226. Phe_am_lyase. 1 hit.
PROSITE	PS00488. PAL_HISTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PAL1_RUBID

Accession

Primary (citable) accession number: Q9M568

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	July 27, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program