Reviewed, UniProtKB/Swiss-Prot P27990 (PALY_MEDSA)

Names and origin

Protein names	Recommended name:     Phenylalanine ammonia-lyase     EC=4.3.1.24
Organism	Medicago sativa (Alfalfa)
Taxonomic identifier	3879 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length	725 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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; cinnamic acid biosynthesis; trans-cinnamic acid from L-phenylalanine: step 1/1.
Subcellular location	Cytoplasm Probable.
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 ligase activity Inferred from electronic annotation. Source: InterPro 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 – 725	725	Phenylalanine ammonia-lyase		PRO_0000215400
Regions
	Compositional bias	24 – 27	4	Poly-Asn
Amino acid modifications
	Modified residue	212	1	2,3-didehydroalanine (Ser) By similarity
	Cross-link	211 ↔ 213		5-imidazolinone (Ala-Gly) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27990-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 19906A2575F64D7D	FASTA	725	78,866
	10 20 30 40 50 60 METISAAITK NNANESFCLI HAKNNNNMKV NEADPLNWGV AAEAMKGSHL DEVKRMVAEY 70 80 90 100 110 120 RKPVVRLGGE TLTISQVAAI AAHDHGVQVD LSESARDGVK ASSEWVMESM NKGTDSYGVT 130 140 150 160 170 180 TGFGATSHSR TKQGGALQKE LIRFLNAGIF GNGTESNHTL PKTATRAAML VRINTLLQGY 190 200 210 220 230 240 SGIDFEILEA ITKPLNKTVT PCLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKAHGPSGEV 250 260 270 280 290 300 LNAKEAFNLA GINAEFFELQ PKEGLALVNG TAVGSGLASI VLFEANILAV LSEVLSAIFA 310 320 330 340 350 360 EVMQGKPEFT DHLTHKLKHH PGQIEAAAIM EHILDGSSYV KAAKKLHEID PLQKPKQDRY 370 380 390 400 410 420 ALRTSPQWLG PLVEVIRFST KSIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVSMDN 430 440 450 460 470 480 TRLALASIGK LMFAQFSELV NDFYNNGLPS NLSASRNPSL DYGFKGAEIA MASYCSELQY 490 500 510 520 530 540 LANPVTTHVQ SAEQHNQDVN SLGLISARKT NEAIEILQLM SSTFLIALCQ AIDLRHLEEN 550 560 570 580 590 600 LKNSVKNTVS QVAKKTLTMG VNGELHPSRF CEKDLLKVVD REHVFAYIDD PCSATYPLSQ 610 620 630 640 650 660 KLRQVLVDHA LVNGESEKNF NTSIFQKIAT FEEELKTLLP KEVESARTAY ESGNPTIPNK 670 680 690 700 710 720 INGCRSYPLY KFVREELGTG LLTGENVISP GEECDKLFSA MCQGKIIDPL LECLGEWNGA PLPIC

References

[1]

"Stress responses in alfalfa (Medicago sativa L.) 12. Sequence analysis of phenylalanine ammonia-lyase (PAL) cDNA clones and appearance of PAL transcripts in elicitor-treated cell cultures and developing plants." Gowri G., Paiva N.L., Dixon R.A. Plant Mol. Biol. 17:415-429(1991) [PubMed: 1715786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Apollo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X58180 mRNA. Translation: CAA41169.1.
PIR	S17444.
3D structure databases
HSSP	HSSP built from PDB template 1GKM based on UniProtKB P21310.
SMR	P27990. Positions 34-725.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.3.1.5. 815.
Family and domain databases
InterPro	IPR001106. Phe/His_NH3-lyase. IPR005922. Phe_NH3-lyase. [Graphical view]
Pfam	PF00221. PAL. 1 hit. [Graphical view]
TIGRFAMs	TIGR01226. phe_am_lyase. 1 hit.
PROSITE	PS00488. PAL_HISTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PALY_MEDSA

Accession

Primary (citable) accession number: P27990

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)