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P25872

- PAL1_TOBAC

UniProt

P25872 - PAL1_TOBAC

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Protein

Phenylalanine ammonia-lyase

Gene

TPA1

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed - 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.

Pathwayi

Sites

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

GO - Molecular functioni

  1. phenylalanine ammonia-lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. cinnamic acid biosynthetic process Source: UniProtKB-UniPathway
  2. L-phenylalanine catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Phenylpropanoid metabolism

Enzyme and pathway databases

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

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
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:
EMBL
GenBank
DDBJ
Links Updated
M84466 Genomic DNA. Translation: AAA34122.1.
AB008200 Genomic DNA. Translation: BAA22948.1.
PIRiS66343.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84466 Genomic DNA. Translation: AAA34122.1 .
AB008200 Genomic DNA. Translation: BAA22948.1 .
PIRi S66343.

3D structure databases

ProteinModelPortali P25872.
SMRi P25872. Positions 21-715.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P25872.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00713 ; UER00725 .
SABIO-RK P25872.

Family and domain databases

Gene3Di 1.10.274.20. 1 hit.
1.10.275.10. 1 hit.
InterProi IPR001106. 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 ]
Pfami PF00221. Lyase_aromatic. 1 hit.
[Graphical view ]
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR01226. phe_am_lyase. 1 hit.
PROSITEi PS00488. PAL_HISTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 91 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