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O24243 (MDL1_PRUDU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
(R)-mandelonitrile lyase 1

EC=4.1.2.10
Alternative name(s):
Hydroxynitrile lyase 1
Short name=(R)-oxynitrilase 1
Gene names
Name:MDL1
OrganismPrunus dulcis (Almond) (Amygdalus dulcis)
Taxonomic identifier3755 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

(R)-mandelonitrile = cyanide + benzaldehyde.

Cofactor

FAD By similarity.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the GMC oxidoreductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 By similarity
Chain28 – 559532(R)-mandelonitrile lyase 1
PRO_0000012344

Regions

Nucleotide binding63 – 642FAD By similarity
Nucleotide binding82 – 832FAD By similarity
Nucleotide binding137 – 1404FAD By similarity
Nucleotide binding486 – 4872FAD By similarity
Nucleotide binding526 – 5272FAD By similarity
Compositional bias293 – 2964Poly-Leu

Sites

Active site4871Proton donor By similarity
Active site5251Proton acceptor By similarity
Binding site1331FAD By similarity
Binding site2441FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site4851Substrate By similarity

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Potential
Glycosylation4671N-linked (GlcNAc...) Potential
Disulfide bond427 ↔ 478 By similarity

Sequences

Sequence LengthMass (Da)Tools
O24243 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 58C2999EBF2E8A54

FASTA55961,100
        10         20         30         40         50         60 
MEKSTMSVIL FVLHLLVLHL QYSEVHSLAN TSAHDFSYLK FVYNATDTSL EGSYDYIVIG 

        70         80         90        100        110        120 
GGTSGCPLAA TLSEKYKVLL LERGTIATEY PNTLTADGFA YNLQQQDDGK TPVERFVSED 

       130        140        150        160        170        180 
GIDNVRARIL GGTTIINAGV YARANISFYS QTGIEWDLDL VNKTYEWVED AIVVKPNNQS 

       190        200        210        220        230        240 
WQSVIGEGFL EAGILPDNGF SLDHEAGTRL TGSTFDNNGT RHAADELLNK GDPNNLLVAV 

       250        260        270        280        290        300 
QASVEKILFS SNTSNLSAIG VIYTDSDGNS HQAFVRGNGE VIVSAGTIGT PQLLLLSGVG 

       310        320        330        340        350        360 
PESYLSSLNI TVVQPNPYVG QFLYNNPRNF INNFPPNPIE ASVVTVLGIR SDYYQVSLSS 

       370        380        390        400        410        420 
LPFSTPPFSL FPTTSYPLPN STFAHIVSQV PGPLSHGSVT LNSSSDVRIA PNIKFNYYSN 

       430        440        450        460        470        480 
STDLANCVSG MKKLGDLLRT KALEPYKARD VLGIDGFNYL GVPLPENQTD DASFETFCLD 

       490        500        510        520        530        540 
NVASYWHYHG GSLVGKVLDD SFRVMGIKAL RVVDASTFPY EPNSHPQGFY LMLGRYVGLQ 

       550 
ILQERSIRLE AIHNIQESM 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08211 mRNA. Translation: CAA69388.1.

3D structure databases

ProteinModelPortalO24243.
SMRO24243. Positions 28-546.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001613. Flavin_amine_oxidase.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFPIRSF000137. Alcohol_oxidase. 1 hit.
PRINTSPR00757. AMINEOXDASEF.
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDL1_PRUDU
AccessionPrimary (citable) accession number: O24243
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families