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O50048

- MDL2_PRUSE

UniProt

O50048 - MDL2_PRUSE

Protein

(R)-mandelonitrile lyase 2

Gene

MDL2

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 75 (01 Oct 2014)
      Sequence version 1 (01 Jun 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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei130 – 1301FAD; via carbonyl oxygenBy similarity
    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 2 (EC:4.1.2.10)
    Alternative name(s):
    Hydroxynitrile lyase 2
    Short name:
    (R)-oxynitrilase 2
    Gene namesi
    Name:MDL2
    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 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 576548(R)-mandelonitrile lyase 2PRO_0000012341Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi428 ↔ 479By similarity
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliO50048.
    SMRiO50048. Positions 29-550.
    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.
    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.

    O50048-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKSTMSAIL VLALHLFVLH LQYSEVQSLA NTSAHDFSYL EFVYDANDTE    50
    LEGTYDYIIV GGGTAGCPLA ATLSANYSVL VLERGTLPTE YPNLLTSDGF 100
    IYNLQQEDDG QTPVERFVSG DGIDNVRGRV LGGTSMINAG VYVRANTSFF 150
    NQTGIEWDMD LVNKTYDWVE DTIVFKPDFQ FWQNLTGTAF LEVGILPDNG 200
    FSLDHLEGTR LTGSTFDNNG TRHASDELLN KGDPNNLRVA VHAAVEKIIF 250
    SSDSSGVTAI GVIYTDSNGT THQAFVRGDG EVILSAGPIG SPQLLLLSGV 300
    GLESYLTSLN ISVVASHPYV GQYIYDNPRN FINILPPNPI EASTVTVLGI 350
    TSDFYQCSIS SLPFSTAPFG FFPNPTYPLP NTTFAHIVNK VPGPLSHGTV 400
    LLQSTSDVRV APNVTFNYYS NTTDLAHCVS GMKKIGEFLS SDALKPYKVE 450
    DLPGIEGFDI LGIPLPENQT DDAAFETFCR EAVASYWHYH GGCLVGEVLD 500
    DDFRVTGINA LRVVDGSTFP STPASHPQGF YLMLGRYMGT KILQERLASE 550
    EALHKSTFEP KILESLESAL SFAFES 576
    Length:576
    Mass (Da):62,724
    Last modified:June 1, 1998 - v1
    Checksum:i570DC7853AE4D3EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF040078 mRNA. Translation: AAB96763.1.
    AF040079 Genomic DNA. Translation: AAB96764.1.
    PIRiT08073.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF040078 mRNA. Translation: AAB96763.1 .
    AF040079 Genomic DNA. Translation: AAB96764.1 .
    PIRi T08073.

    3D structure databases

    ProteinModelPortali O50048.
    SMRi O50048. Positions 29-550.
    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. Hu Z., Poulton J.E.
      Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

    Entry informationi

    Entry nameiMDL2_PRUSE
    AccessioniPrimary (citable) accession number: O50048
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 75 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