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P25872 (PAL1_TOBAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenylalanine ammonia-lyase

EC=4.3.1.24
Gene names
Name:TPA1
Synonyms:PALB
OrganismNicotiana tabacum (Common tobacco)
Taxonomic identifier4097 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Protein attributes

Sequence length715 AA.
Sequence statusComplete.
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; trans-cinnamate biosynthesis; trans-cinnamate from L-phenylalanine: step 1/1.

Subcellular location

Cytoplasm Probable.

Tissue specificity

Expressed in flowers, roots, leaves and stems. Ref.1

Developmental stage

Expression declines during flower maturation but increases during leaf maturation.

Induction

Rapidly induced after wounding. Ref.1

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

cinnamic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphenylalanine ammonia-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 715715Phenylalanine ammonia-lyase
PRO_0000215423

Amino acid modifications

Modified residue20212,3-didehydroalanine (Ser) By similarity
Cross-link201 ↔ 2035-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence LengthMass (Da)Tools
P25872 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 03CB4E8527394C62

FASTA71577,781
        10         20         30         40         50         60 
MASNGHVNGG ENFELCKKSA DPLNWEMAAE SLRGSHLDEV KKMVSEFRKP MVKLGGESLT 

        70         80         90        100        110        120 
VAQVAAIAVR DKSANGVKVE LSEEARAGVK ASSDWVMDSM NKGTDSYGVT TGFGATSHRR 

       130        140        150        160        170        180 
TKNGGALQKE LIRFLNAGVF GNGTETSHTL PHSATRAAML VRINTLLQGY SGIRFEILEA 

       190        200        210        220        230        240 
ITKLINSNIT PCLPLRGTIT ASGDLVPLSY IAGLLTGRPN SKAVGPNGET LNAEEAFRVA 

       250        260        270        280        290        300 
GVNGGFFELQ PKEGLALVNG TAVGSGMASM VLFDSNILAV MSEVLSAIFA EVMNGKPEFT 

       310        320        330        340        350        360 
DHLTHKLKHH PGQIEAAAIM EHILDGSSYV KAAQKLHEMD PLQKPKQDRY ALRTSPQWLG 

       370        380        390        400        410        420 
PQIEVIRAAT KMIEREINSV NDNPLIDVSR NKALHGGNFQ GTPIGVSMDN ARLALASIGK 

       430        440        450        460        470        480 
LMFAQFSELV NDYYNNGLPS NLTASRNPSL DYGFKGAEIA MASYCSELQF LANPVTNHVQ 

       490        500        510        520        530        540 
SAEQHNQDVN SLGLISARKT AEAVDILKLM SSTYLVALCQ AIDLRHLEEN LKNAVKNTVS 

       550        560        570        580        590        600 
QVAKRTLTMG ANGELHPARF CEKELLRIVD REYLFAYADD PCSCNYPLMQ KLRQVLVDHA 

       610        620        630        640        650        660 
MNNGESEKNV NSSIFQKIGA FEDELKAVLP KEVESARAAL ESGNPAIPNR ITECRSYPLY 

       670        680        690        700        710 
RFVRKELGTE LLTGEKVRSP GEECDKVFTA MCNGQIIDPM LECLKSWNGA PLPIC 

« Hide

References

[1]"Phenylalanine ammonia-lyase gene structure, expression, and evolution in Nicotiana."
Fukasawa-Akada T., Kung S.D., Watson J.C.
Plant Mol. Biol. 30:711-722(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
[2]Taguchi G., Sharan M., Gonda K., Yanagisawa K., Shimosaka M., Hayashida N., Okazaki M.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Bright Yellow.
Tissue: Callus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84466 Genomic DNA. Translation: AAA34122.1.
AB008200 Genomic DNA. Translation: BAA22948.1.
PIRS66343.

3D structure databases

ProteinModelPortalP25872.
SMRP25872. Positions 21-715.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP25872.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP25872.
UniPathwayUPA00713; UER00725.

Family and domain databases

Gene3D1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
IPR005922. Phe_NH3-lyase.
IPR023144. Phe_NH3-lyase_shielding_dom.
[Graphical view]
PfamPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR01226. phe_am_lyase. 1 hit.
PROSITEPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePAL1_TOBAC
AccessionPrimary (citable) accession number: P25872
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: February 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways