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Protein

Phenylalanine ammonia-lyase

Gene

TPA1

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

L-phenylalanine = trans-cinnamate + ammonia.

Pathway:itrans-cinnamate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes trans-cinnamate from L-phenylalanine.
Proteins known to be involved in this subpathway in this organism are:
  1. Phenylalanine ammonia-lyase (pal4), Phenylalanine ammonia-lyase (NtPAL), Phenylalanine ammonia-lyase (TPA1), Phenylalanine ammonia-lyase (PALA), Phenylalanine ammonia-lyase
This subpathway is part of the pathway trans-cinnamate biosynthesis, which is itself part of Phenylpropanoid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes trans-cinnamate from L-phenylalanine, the pathway trans-cinnamate biosynthesis and in Phenylpropanoid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei107 – 1071Proton donor/acceptorBy similarity
Binding sitei353 – 3531SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Phenylpropanoid metabolism

Enzyme and pathway databases

BRENDAi4.3.1.24. 3645.
SABIO-RKP25872.
UniPathwayiUPA00713; UER00725.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine ammonia-lyase (EC:4.3.1.24)
Gene namesi
Name:TPA1
Synonyms:PALB
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Phenylalanine ammonia-lyasePRO_0000215423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki201 ↔ 2035-imidazolinone (Ala-Gly)By similarity
Modified residuei202 – 20212,3-didehydroalanine (Ser)PROSITE-ProRule annotation

Post-translational modificationi

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

Proteomic databases

PRIDEiP25872.

Expressioni

Tissue specificityi

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

Developmental stagei

Expression declines during flower maturation but increases during leaf maturation.

Inductioni

Rapidly induced after wounding.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP25872.
SMRiP25872. Positions 21-715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Family and domain databases

Gene3Di1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProiIPR001106. 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]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01226. phe_am_lyase. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNGHVNGG ENFELCKKSA DPLNWEMAAE SLRGSHLDEV KKMVSEFRKP
60 70 80 90 100
MVKLGGESLT VAQVAAIAVR DKSANGVKVE LSEEARAGVK ASSDWVMDSM
110 120 130 140 150
NKGTDSYGVT TGFGATSHRR TKNGGALQKE LIRFLNAGVF GNGTETSHTL
160 170 180 190 200
PHSATRAAML VRINTLLQGY SGIRFEILEA ITKLINSNIT PCLPLRGTIT
210 220 230 240 250
ASGDLVPLSY IAGLLTGRPN SKAVGPNGET LNAEEAFRVA GVNGGFFELQ
260 270 280 290 300
PKEGLALVNG TAVGSGMASM VLFDSNILAV MSEVLSAIFA EVMNGKPEFT
310 320 330 340 350
DHLTHKLKHH PGQIEAAAIM EHILDGSSYV KAAQKLHEMD PLQKPKQDRY
360 370 380 390 400
ALRTSPQWLG PQIEVIRAAT KMIEREINSV NDNPLIDVSR NKALHGGNFQ
410 420 430 440 450
GTPIGVSMDN ARLALASIGK LMFAQFSELV NDYYNNGLPS NLTASRNPSL
460 470 480 490 500
DYGFKGAEIA MASYCSELQF LANPVTNHVQ SAEQHNQDVN SLGLISARKT
510 520 530 540 550
AEAVDILKLM SSTYLVALCQ AIDLRHLEEN LKNAVKNTVS QVAKRTLTMG
560 570 580 590 600
ANGELHPARF CEKELLRIVD REYLFAYADD PCSCNYPLMQ KLRQVLVDHA
610 620 630 640 650
MNNGESEKNV NSSIFQKIGA FEDELKAVLP KEVESARAAL ESGNPAIPNR
660 670 680 690 700
ITECRSYPLY RFVRKELGTE LLTGEKVRSP GEECDKVFTA MCNGQIIDPM
710
LECLKSWNGA PLPIC
Length:715
Mass (Da):77,781
Last modified:May 1, 1992 - v1
Checksum:i03CB4E8527394C62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84466 Genomic DNA. Translation: AAA34122.1.
AB008200 Genomic DNA. Translation: BAA22948.1.
PIRiS66343.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84466 Genomic DNA. Translation: AAA34122.1.
AB008200 Genomic DNA. Translation: BAA22948.1.
PIRiS66343.

3D structure databases

ProteinModelPortaliP25872.
SMRiP25872. Positions 21-715.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP25872.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00713; UER00725.
BRENDAi4.3.1.24. 3645.
SABIO-RKP25872.

Family and domain databases

Gene3Di1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProiIPR001106. 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]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01226. phe_am_lyase. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPAL1_TOBAC
AccessioniPrimary (citable) accession number: P25872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 1, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.