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Reviewed, UniProtKB/Swiss-Prot Q42858 (PAL2_IPOBA)

Last modified June 16, 2009. Version 59. 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
OrganismIpomoea batatas (Sweet potato) (Batate)
Taxonomic identifier4120 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesConvolvulaceaeIpomoeeaeIpomoea

Protein attributes

Sequence length708 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 – 708708Phenylalanine ammonia-lyase
PRO_0000215394

Amino acid modifications

Modified residue19512,3-didehydroalanine (Ser) By similarity
Cross-link194 ↔ 1965-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q42858-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C10F736C41F1BEC6

FASTA70877,383
        10         20         30         40         50         60 
MEGAIANGHT NDFCIKVDPL NWEMAADSLK GSHLDEVKRM VAEFRNPAVK IGGQTLTSLR 

        70         80         90        100        110        120 
SPPIAARDNA SKWSSPRLPA RRESSSDWVM NSMNNGTDSY GVTTGFGATS HRRTKNGHAL 

       130        140        150        160        170        180 
QQELIRFLNA GIFGTGTGAS HTLPHSATRA AMLVRINTLL QGYSGIRFEI LEAITKLLNH 

       190        200        210        220        230        240 
NITPCLPLRG TITASGDLVP LSYIAGLLTG RPNSKAVGPN GEALTAEEAF KLAGVQGGFF 

       250        260        270        280        290        300 
ELQPKEGLAL VNGTAVGSGM ASMVLFEANV LAVLSEVLSA IFAEVMNGKP EFTDHLTHKL 

       310        320        330        340        350        360 
KHHPGQIEAA AIMEHILDRS YYMKAAQKLH EMDPLQKPKQ DRYALRTSPQ WLGPQIEVIR 

       370        380        390        400        410        420 
QATKMIEREI NSVNDNPLID VSRNKALHGG NFQGTPIGVS MDNSRLALAS IGKLIFAQFS 

       430        440        450        460        470        480 
ELVNDYYNNG LPSNLTAGRN PSLDYGFKGV EIAMASYCSE LQFLANPVTN HVQSAEQHNQ 

       490        500        510        520        530        540 
DVNSLGLISA RKTAEAVDVL KLMSSTYLVA LCQAIDLRHL EENLKNAVRN TVNQVAKRTL 

       550        560        570        580        590        600 
TMGVNGELHP SRFCEKDLLR VVDREYVFAY ADDPCSANYP LFQKLRQVLV DHALQNGEHE 

       610        620        630        640        650        660 
KNVSTSIFQK IAAFEDELKA VLPKEVEGAR SAIENGNPAI PNRITECRSY PLYKFVREEL 

       670        680        690        700 
GTEMLTGEKV KSPGEVCDKV FTAVCDGGII DPLLECLKSW DGAPLPIC 

« Hide

References

[1]Tanaka Y.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Beniazuma.
Tissue: Root.

Cross-references

Sequence databases

D78640 mRNA. Translation: BAA11459.1.
PIRT10909.

3D structure databases

HSSPHSSP built from PDB template 1GKM based on UniProtKB P21310.
SMRQ42858. Positions 18-708.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.3.1.5. 21210.

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 namePAL2_IPOBA
AccessionPrimary (citable) accession number: Q42858
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 59 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