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P25872

- PAL1_TOBAC

UniProt

P25872 - PAL1_TOBAC

Protein

Phenylalanine ammonia-lyase

Gene

TPA1

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    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

    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-SubCell

    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

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    MASNGHVNGG ENFELCKKSA DPLNWEMAAE SLRGSHLDEV KKMVSEFRKP    50
    MVKLGGESLT VAQVAAIAVR DKSANGVKVE LSEEARAGVK ASSDWVMDSM 100
    NKGTDSYGVT TGFGATSHRR TKNGGALQKE LIRFLNAGVF GNGTETSHTL 150
    PHSATRAAML VRINTLLQGY SGIRFEILEA ITKLINSNIT PCLPLRGTIT 200
    ASGDLVPLSY IAGLLTGRPN SKAVGPNGET LNAEEAFRVA GVNGGFFELQ 250
    PKEGLALVNG TAVGSGMASM VLFDSNILAV MSEVLSAIFA EVMNGKPEFT 300
    DHLTHKLKHH PGQIEAAAIM EHILDGSSYV KAAQKLHEMD PLQKPKQDRY 350
    ALRTSPQWLG PQIEVIRAAT KMIEREINSV NDNPLIDVSR NKALHGGNFQ 400
    GTPIGVSMDN ARLALASIGK LMFAQFSELV NDYYNNGLPS NLTASRNPSL 450
    DYGFKGAEIA MASYCSELQF LANPVTNHVQ SAEQHNQDVN SLGLISARKT 500
    AEAVDILKLM SSTYLVALCQ AIDLRHLEEN LKNAVKNTVS QVAKRTLTMG 550
    ANGELHPARF CEKELLRIVD REYLFAYADD PCSCNYPLMQ KLRQVLVDHA 600
    MNNGESEKNV NSSIFQKIGA FEDELKAVLP KEVESARAAL ESGNPAIPNR 650
    ITECRSYPLY RFVRKELGTE LLTGEKVRSP GEECDKVFTA MCNGQIIDPM 700
    LECLKSWNGA PLPIC 715
    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 1, 2014
    This is version 90 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