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O82784

- MDL4_PRUSE

UniProt

O82784 - MDL4_PRUSE

Protein

(R)-mandelonitrile lyase 4

Gene

MDL4

Organism
Prunus serotina (Black cherry)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. It is a major seed constituent, and could have the additional role of a storage form for reduced nitrogen By similarity.By similarity

    Catalytic activityi

    (R)-mandelonitrile = cyanide + benzaldehyde.

    Cofactori

    FAD.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei134 – 1341FADBy similarity
    Binding sitei245 – 2451FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei357 – 3571SubstrateBy similarity
    Binding sitei486 – 4861SubstrateBy similarity
    Active sitei488 – 4881Proton donorBy similarity
    Binding sitei516 – 5161FAD; via amide nitrogenBy similarity
    Active sitei526 – 5261Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi64 – 652FADBy similarity
    Nucleotide bindingi83 – 842FADBy similarity
    Nucleotide bindingi138 – 1414FADBy similarity
    Nucleotide bindingi487 – 4882FADBy similarity
    Nucleotide bindingi527 – 5282FADBy similarity

    GO - Molecular functioni

    1. choline dehydrogenase activity Source: InterPro
    2. flavin adenine dinucleotide binding Source: InterPro
    3. mandelonitrile lyase activity Source: UniProtKB-EC

    GO - Biological processi

    1. alcohol metabolic process Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    (R)-mandelonitrile lyase 4 (EC:4.1.2.10)
    Alternative name(s):
    Hydroxynitrile lyase 4
    Short name:
    (R)-oxynitrilase 4
    Gene namesi
    Name:MDL4
    OrganismiPrunus serotina (Black cherry)
    Taxonomic identifieri23207 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

    Subcellular locationi

    Vacuolealeurone grain By similarity
    Note: Primarily found within protein bodies of the cotyledonary parenchyma cells, with lesser amounts within the procambium.By similarity

    GO - Cellular componenti

    1. aleurone grain Source: UniProtKB-SubCell
    2. vacuole Source: UniProtKB-KW

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 574547(R)-mandelonitrile lyase 4PRO_0000012343Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi428 ↔ 479By similarity
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO82784.
    SMRiO82784. Positions 31-549.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi294 – 2974Poly-Leu

    Sequence similaritiesi

    Belongs to the GMC oxidoreductase family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR012132. GMC_OxRdtase.
    IPR000172. GMC_OxRdtase_N.
    IPR007867. GMC_OxRtase_C.
    [Graphical view]
    PfamiPF05199. GMC_oxred_C. 1 hit.
    PF00732. GMC_oxred_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
    PROSITEiPS00624. GMC_OXRED_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O82784-1 [UniParc]FASTAAdd to Basket

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    MEKSTMSAVV LVLNLLVLHL QYSEVHSLAN TSSEHDFGYL KFVYNAVDLE    50
    LEGSYDYIIV GGGTSGCPLA ATLSANYSVL VLERGTIATE YPNTLTVDGF 100
    AYNLQQQDDG KTPVERFVSE DGIDNVRSRI LGGTTIINAG VYARANESFY 150
    NNSGVEWDLD LVNEAYEWVE DAIVYKPSNQ SWQSITGTAF LEAGVHPDNG 200
    FGLVHEEGTR LTGSTFDNSG TRHASDELLN KGDPDNLKVA VEAAVQKIIF 250
    STESSGLTAV GVVYTDSNGT SHRALVSGKG EVILSAGTLG TPQLLLLSGV 300
    GPESYLTSLN ISVVASHPYV GQYVNDNPRN FINILPPNPI EPSTVTVLGI 350
    TSDFYQCSLS SLPFDTPPFS LFPTTSYPLP NQTFAHIVSK VPGPLSAGSL 400
    TLQSSSNVSV APNVKFNYCS DPVDLTHCVS GMKKIGVFLS TDALKPYKVD 450
    DLPGIDGFNI LGTPLPENQT DDAAFEKFCR DTVASYWHYH GGAIVGKVID 500
    GNFRVTGINA LRVVDGSTFP ATPASHPQGF YLMLGRYVGT KIVQERSASG 550
    EAIHTSTFKP KLMDSLKSAL SFAF 574
    Length:574
    Mass (Da):61,682
    Last modified:November 1, 1998 - v1
    Checksum:iBCDFAE1DC5D2C539
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043186 mRNA. Translation: AAD02265.1.
    AF043187 Genomic DNA. Translation: AAD02266.1.
    AF053884 mRNA. Translation: AAC61980.1.
    AF053885 Genomic DNA. Translation: AAC61981.1.
    PIRiT50766.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF043186 mRNA. Translation: AAD02265.1 .
    AF043187 Genomic DNA. Translation: AAD02266.1 .
    AF053884 mRNA. Translation: AAC61980.1 .
    AF053885 Genomic DNA. Translation: AAC61981.1 .
    PIRi T50766.

    3D structure databases

    ProteinModelPortali O82784.
    SMRi O82784. Positions 31-549.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR012132. GMC_OxRdtase.
    IPR000172. GMC_OxRdtase_N.
    IPR007867. GMC_OxRtase_C.
    [Graphical view ]
    Pfami PF05199. GMC_oxred_C. 1 hit.
    PF00732. GMC_oxred_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000137. Alcohol_oxidase. 1 hit.
    PROSITEi PS00624. GMC_OXRED_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Hu Z., Poulton J.E.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

    Entry informationi

    Entry nameiMDL4_PRUSE
    AccessioniPrimary (citable) accession number: O82784
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3