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O24243

- MDL1_PRUDU

UniProt

O24243 - MDL1_PRUDU

Protein

(R)-mandelonitrile lyase 1

Gene

MDL1

Organism
Prunus dulcis (Almond) (Amygdalus dulcis)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Jan 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 sitei133 – 1331FADBy similarity
    Binding sitei244 – 2441FAD; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei485 – 4851SubstrateBy similarity
    Active sitei487 – 4871Proton donorBy 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 1 (EC:4.1.2.10)
    Alternative name(s):
    Hydroxynitrile lyase 1
    Short name:
    (R)-oxynitrilase 1
    Gene namesi
    Name:MDL1
    OrganismiPrunus dulcis (Almond) (Amygdalus dulcis)
    Taxonomic identifieri3755 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727By similarityAdd
    BLAST
    Chaini28 – 559532(R)-mandelonitrile lyase 1PRO_0000012344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi255 – 2551N-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.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO24243.
    SMRiO24243. Positions 28-546.
    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

    InterProiIPR001613. Flavin_amine_oxidase.
    IPR012132. 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.
    PRINTSiPR00757. AMINEOXDASEF.
    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.

    O24243-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKSTMSVIL FVLHLLVLHL QYSEVHSLAN TSAHDFSYLK FVYNATDTSL    50
    EGSYDYIVIG GGTSGCPLAA TLSEKYKVLL LERGTIATEY PNTLTADGFA 100
    YNLQQQDDGK TPVERFVSED GIDNVRARIL GGTTIINAGV YARANISFYS 150
    QTGIEWDLDL VNKTYEWVED AIVVKPNNQS WQSVIGEGFL EAGILPDNGF 200
    SLDHEAGTRL TGSTFDNNGT RHAADELLNK GDPNNLLVAV QASVEKILFS 250
    SNTSNLSAIG VIYTDSDGNS HQAFVRGNGE VIVSAGTIGT PQLLLLSGVG 300
    PESYLSSLNI TVVQPNPYVG QFLYNNPRNF INNFPPNPIE ASVVTVLGIR 350
    SDYYQVSLSS LPFSTPPFSL FPTTSYPLPN STFAHIVSQV PGPLSHGSVT 400
    LNSSSDVRIA PNIKFNYYSN STDLANCVSG MKKLGDLLRT KALEPYKARD 450
    VLGIDGFNYL GVPLPENQTD DASFETFCLD NVASYWHYHG GSLVGKVLDD 500
    SFRVMGIKAL RVVDASTFPY EPNSHPQGFY LMLGRYVGLQ ILQERSIRLE 550
    AIHNIQESM 559
    Length:559
    Mass (Da):61,100
    Last modified:January 1, 1998 - v1
    Checksum:i58C2999EBF2E8A54
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08211 mRNA. Translation: CAA69388.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08211 mRNA. Translation: CAA69388.1 .

    3D structure databases

    ProteinModelPortali O24243.
    SMRi O24243. Positions 28-546.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR001613. Flavin_amine_oxidase.
    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.
    PRINTSi PR00757. AMINEOXDASEF.
    PROSITEi PS00623. GMC_OXRED_1. 1 hit.
    PS00624. GMC_OXRED_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Suelves M.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Texas.
      Tissue: Flower.

    Entry informationi

    Entry nameiMDL1_PRUDU
    AccessioniPrimary (citable) accession number: O24243
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 73 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