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P52707

- MDL3_PRUSE

UniProt

P52707 - MDL3_PRUSE

Protein

(R)-mandelonitrile lyase 3

Gene

MDL3

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 78 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.

    Catalytic activityi

    (R)-mandelonitrile = cyanide + benzaldehyde.

    Cofactori

    FAD.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei129 – 1291FAD; via carbonyl oxygenBy similarity
    Binding sitei133 – 1331FADBy similarity
    Binding sitei244 – 2441FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei356 – 3561SubstrateBy similarity
    Binding sitei485 – 4851SubstrateBy similarity
    Active sitei487 – 4871Proton donorBy similarity
    Binding sitei515 – 5151FAD; via amide nitrogenBy similarity
    Active sitei525 – 5251Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi63 – 642FADBy similarity
    Nucleotide bindingi82 – 832FADBy similarity
    Nucleotide bindingi137 – 1404FADBy similarity
    Nucleotide bindingi486 – 4872FADBy similarity
    Nucleotide bindingi526 – 5272FADBy 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 3 (EC:4.1.2.10)
    Alternative name(s):
    Hydroxynitrile lyase 3
    Short name:
    (R)-oxynitrilase 3
    Gene namesi
    Name:MDL3
    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 – 573546(R)-mandelonitrile lyase 3PRO_0000012342Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi420 – 4201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi427 ↔ 478By similarity
    Glycosylationi467 – 4671N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliP52707.
    SMRiP52707. Positions 28-549.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi293 – 2964Poly-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.
    PROSITEiPS00623. GMC_OXRED_1. 1 hit.
    PS00624. GMC_OXRED_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P52707-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKSTMSAVL LVLHIFVLHL QYSEVQSLAN TSSHDFSYLS FVYDATDPEL    50
    EGSYDYIIVG GGTAGCPLAA TLSANYSVLV LERGSLPTEY PNLLISDGFV 100
    YNLQQEDDGK TPVERFVSED GIDNVRGRVL GGTSMINAGV YVRANTSFFN 150
    QTGIEWDMDL VNQTYEWVED TIVFEPDSQT WQTVIGTAYL EAGILPNNGF 200
    SVDHLAGTRL TGSTFDNNGT RHASDELLNK GDPNNLRVAV QAAVEKIIFS 250
    SNTSGVTAIG VIYTDSNGTT HQAFVRGEGE VILSAGPIGS PQLLLLSGVG 300
    PESYLTSLNI SVVASHPYVG QYIYDNPRNF INILPPNPIE ASTVTVLGIT 350
    SDFYQCSISS LPFDTPPFSF FPTTSYPLPN QTFAHIVNKV PGPLSHGTVT 400
    LNSSSDVRVG PNVKFNYYSN LTDLSHCVSG MKKLGEVLST DALEPYKVED 450
    LPGIDGFNIL GIPLPENQTD DAAFETFCRE SVASYWHYHG GCLVGKVLDD 500
    GFRVTGINAL RVVDGSTFPS TPASHPQGFY LMLGRYMGIQ ILQERSASED 550
    AIRNLGFQEN ILDSPKSTSS FAF 573
    Length:573
    Mass (Da):62,180
    Last modified:October 1, 1996 - v1
    Checksum:iDB181C68FED3F800
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51562 Genomic DNA. Translation: AAA96782.1.
    AF013161 mRNA. Translation: AAB67714.1.
    PIRiT07948.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U51562 Genomic DNA. Translation: AAA96782.1 .
    AF013161 mRNA. Translation: AAB67714.1 .
    PIRi T07948.

    3D structure databases

    ProteinModelPortali P52707.
    SMRi P52707. Positions 28-549.
    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 PS00623. GMC_OXRED_1. 1 hit.
    PS00624. GMC_OXRED_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing, genomic organization, and preliminary promoter analysis of a black cherry (R)-(+)-mandelonitrile lyase gene."
      Hu Z., Poulton J.E.
      Plant Physiol. 115:1359-1369(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

    Entry informationi

    Entry nameiMDL3_PRUSE
    AccessioniPrimary (citable) accession number: P52707
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 78 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