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Q9FV54

- DEF1B_SOLLC

UniProt

Q9FV54 - DEF1B_SOLLC

Protein

Peptide deformylase 1B, chloroplastic

Gene

PDF1B

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Removes the formyl group from the N-terminal Met of newly synthesized proteins.By similarity

    Catalytic activityi

    Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.

    Cofactori

    Binds 1 Fe2+ ion.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi177 – 1771IronBy similarity
    Metal bindingi219 – 2191IronBy similarity
    Active sitei220 – 2201By similarity
    Metal bindingi223 – 2231IronBy similarity

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. peptide deformylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    SABIO-RKQ9FV54.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptide deformylase 1B, chloroplastic (EC:3.5.1.88)
    Short name:
    PDF 1B
    Alternative name(s):
    Polypeptide deformylase
    Gene namesi
    Name:PDF1B
    OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
    Taxonomic identifieri4081 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
    ProteomesiUP000004994: Chromosome 2

    Subcellular locationi

    Plastidchloroplast Curated

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 279Peptide deformylase 1B, chloroplasticPRO_0000006733
    Transit peptidei1 – ?ChloroplastSequence Analysis

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FV54.
    SMRiQ9FV54. Positions 80-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the polypeptide deformylase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KOiK01462.
    OMAiFFDRMTE.

    Family and domain databases

    Gene3Di3.90.45.10. 1 hit.
    HAMAPiMF_00163. Pep_deformylase.
    InterProiIPR000181. Fmet_deformylase.
    IPR023635. Peptide_deformylase.
    [Graphical view]
    PANTHERiPTHR10458. PTHR10458. 1 hit.
    PfamiPF01327. Pep_deformylase. 1 hit.
    [Graphical view]
    PRINTSiPR01576. PDEFORMYLASE.
    SUPFAMiSSF56420. SSF56420. 1 hit.
    TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9FV54-1 [UniParc]FASTAAdd to Basket

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    MAMAAASWAS SSSFTRFLRP LLSRNSSPSP ISYSLHRYKS ANCLFFSASS    50
    NKPPKLAVYA QARRVLSSKT KGDEIATPAD LSFVVPLKIV EYPDPILRAK 100
    NKRIDNFDAN LKKLVDEMFD IMYKTDGIGL SAPQVGMNVQ LMVFNAAGER 150
    GEGEEIVLVN PRVSRYSRRI IPYEEGCLSF PMIHGDVKRP ESVKVDAQDI 200
    NGTRFEISLS ALPARVFQHE FDHLQGVLFF DKMTDEVLDT IREKLVALEK 250
    KYEDRTGLPT PESINTRKIK KAAVGFGKS 279
    Length:279
    Mass (Da):31,197
    Last modified:March 1, 2001 - v1
    Checksum:i750F6406FDAC4233
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250958 mRNA. Translation: AAG33972.1.
    RefSeqiNP_001234441.1. NM_001247512.1.
    UniGeneiLes.3729.

    Genome annotation databases

    EnsemblPlantsiSolyc02g086680.2.1; Solyc02g086680.2.1; Solyc02g086680.2.
    GeneIDi543648.
    KEGGisly:543648.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF250958 mRNA. Translation: AAG33972.1 .
    RefSeqi NP_001234441.1. NM_001247512.1.
    UniGenei Les.3729.

    3D structure databases

    ProteinModelPortali Q9FV54.
    SMRi Q9FV54. Positions 80-262.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi Solyc02g086680.2.1 ; Solyc02g086680.2.1 ; Solyc02g086680.2 .
    GeneIDi 543648.
    KEGGi sly:543648.

    Phylogenomic databases

    KOi K01462.
    OMAi FFDRMTE.

    Enzyme and pathway databases

    SABIO-RK Q9FV54.

    Family and domain databases

    Gene3Di 3.90.45.10. 1 hit.
    HAMAPi MF_00163. Pep_deformylase.
    InterProi IPR000181. Fmet_deformylase.
    IPR023635. Peptide_deformylase.
    [Graphical view ]
    PANTHERi PTHR10458. PTHR10458. 1 hit.
    Pfami PF01327. Pep_deformylase. 1 hit.
    [Graphical view ]
    PRINTSi PR01576. PDEFORMYLASE.
    SUPFAMi SSF56420. SSF56420. 1 hit.
    TIGRFAMsi TIGR00079. pept_deformyl. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms."
      Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.
      EMBO J. 19:5916-5929(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiDEF1B_SOLLC
    AccessioniPrimary (citable) accession number: Q9FV54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3