NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Apollo;
DOI=10.1007/BF00040636; PubMed=1715786 [NCBI, ExPASy, EBI, Israel, Japan]
Gowri G., Paiva N.L., Dixon R.A.;
"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.";
Plant Mol. Biol. 17:415-429(1991).

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).
PTM: 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).
SIMILARITY: Belongs to the PAL/histidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X58180; CAA41169.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17444; S17444.

3D structure databases

HSSP

P21310; 1GKM. [HSSP ENTRY / PDB]

SMR

P27990; 34-725.

ModBase

P27990.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0016211;	Molecular function: ammonia ligase activity (inferred from electronic annotation from InterPro).
GO:0016841;	Molecular function: ammonia-lyase activity (inferred from electronic annotation from InterPro).
GO:0009058;	Biological process: biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006559;	Biological process: L-phenylalanine catabolic process (inferred from electronic annotation from InterPro).
GO:0009698;	Biological process: phenylpropanoid metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001106; Phe/His_NH3-lyase.
IPR005922; Phe_NH3-lyase.
Graphical view of domain structure.

Pfam

PF00221; PAL; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01226; phe_am_lyase; 1.

PROSITE

PS00488; PAL_HISTIDASE; 1.

Other

ProtoNet

P27990.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Lyase; Phenylpropanoid metabolism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 725`	`725`	`Phenylalanine ammonia-lyase.`	`PRO_0000215400`
`COMPBIAS`	`24 27`	`4`	`Poly-Asn.`
`MOD_RES`	`212 212`		`2,3-didehydroalanine (Ser) (By similarity).`
`CROSSLNK`	`211 213`		`5-imidazolinone (Ala-Gly) (By similarity).`

Sequence information

Length: 725 AA [This is the length of the unprocessed precursor]

Molecular weight: 78866 Da [This is the MW of the unprocessed precursor]

CRC64: 19906A2575F64D7D [This is a checksum on the sequence]

        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

P27990 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools