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Reviewed, UniProtKB/Swiss-Prot Q42667 (PALY_CITLI)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phenylalanine ammonia-lyase
    EC=4.3.1.24
Gene names
Name: PAL6
OrganismCitrus limon (Lemon)
Taxonomic identifier2708 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IISapindalesRutaceaeCitrus

Protein attributes

Sequence length722 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 processPhenylpropanoid metabolism
   Cellular componentCytoplasm
   Molecular functionLyase
Gene Ontology (GO)
   Biological processL-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 componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionammonia ligase activity

Inferred from electronic annotation. Source: InterPro

ammonia-lyase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 722722Phenylalanine ammonia-lyase
PRO_0000215389

Amino acid modifications

Modified residue20712,3-didehydroalanine (Ser) By similarity
Cross-link206 ↔ 2085-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q42667-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C96893196E30D9E5

FASTA72278,490
        10         20         30         40         50         60 
MELSHETCNG IKNDRNGGTS SLGLCTGTDP LNWTVAADSL KGSHLDEVKR MIDEYRRPVV 

        70         80         90        100        110        120 
KLGGESLTIG QVTAIAAHDS GVKVELAEAA RAGVKASSDW VMDSMMKGTD SYGVTTGFGA 

       130        140        150        160        170        180 
TSHRRTKQGG ALQKELIRFL NSGIFGNGTE SSHTLPHSAT RAAMLVRVNT LLQGYSGIRF 

       190        200        210        220        230        240 
EILETITKFL NHNITPCLPL RGTITASGDL VPLSYIAGLL TGRPNSKAVG SNGQVLNPTE 

       250        260        270        280        290        300 
AFNLAGVTSG FFELQPKEGL ALVNGTAVGS GLAATVLFEA NILAIMSEVL SAIFAEVMNG 

       310        320        330        340        350        360 
KPEFTDHLTH KLKHHPGQIE AAAIMEHILD GSSYVKAAQK LHETDPLQKP KQDRYALRTS 

       370        380        390        400        410        420 
PQWLGPQIEV IRAATKMIER EINSVNDNPL IDVSRNKALH GGNFQGTPIG VSMDNTRLAI 

       430        440        450        460        470        480 
ASIGKLMFAQ FSELVNDFYN NGLPSNLTGG RNPSLDYGFK GAEIAMASYC SELQFLANPV 

       490        500        510        520        530        540 
TNHVQSAEQH NQDVNSLGLN SSRKTAEAVD ILKLMSSTFL VALCQAIDLR HLEENLKNTV 

       550        560        570        580        590        600 
KNTVSQVAKR VLTMGVNGEL HPSRFCEKDL IKVVDREYVF AYIDDPCSAS SPLMQKLRQV 

       610        620        630        640        650        660 
LVDHALDNGD REKNSTTSIF QKIGAFEDEL KTLLPKEVEI ARTELESGNA AIPNRIKECR 

       670        680        690        700        710        720 
SYPLYKIVRE DIGTSLLTGE KVRSPGEEFD KVFTAMCEGK LIDPMLECLK EWNGAPLPIC 


QN 

« Hide

References

[1]"A full-length cDNA coding for phenylalanine ammonia-lyase from Citrus limon."
Seelenfreund D., Chiong M., Lobos S., Perez L.M.
Plant Gene Register PGR96-026
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

U43338 mRNA. Translation: AAB67733.1.

3D structure databases

HSSPHSSP built from PDB template 1GK2 based on UniProtKB P21310.
SMRQ42667. Positions 29-720.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.3.1.5. 66695.

Family and domain databases

InterProIPR001106. Phe/His_NH3-lyase.
IPR005922. Phe_NH3-lyase.
[Graphical view]
PfamPF00221. PAL. 1 hit.
[Graphical view]
TIGRFAMsTIGR01226. phe_am_lyase. 1 hit.
PROSITEPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePALY_CITLI
AccessionPrimary (citable) accession number: Q42667
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents