Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P52707 (MDL3_PRUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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 3

EC=4.1.2.10
Alternative name(s):
Hydroxynitrile lyase 3
Short name=(R)-oxynitrilase 3
Gene names
Name:MDL3
OrganismPrunus serotina (Black cherry)
Taxonomic identifier23207 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

Protein attributes

Sequence length573 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.

Catalytic activity

(R)-mandelonitrile = cyanide + benzaldehyde.

Cofactor

FAD.

Subunit structure

Monomer.

Subcellular location

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

Sequence similarities

Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   LigandFAD
Flavoprotein
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological_processalcohol metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentaleurone grain

Inferred from electronic annotation. Source: UniProtKB-SubCell

vacuole

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncholine dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

mandelonitrile lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 573546(R)-mandelonitrile lyase 3
PRO_0000012342

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 site1291FAD; via carbonyl oxygen By similarity
Binding site1331FAD By similarity
Binding site2441FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3561Substrate By similarity
Binding site4851Substrate By similarity
Binding site5151FAD; via amide nitrogen By similarity

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1621N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation2671N-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
P52707 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DB181C68FED3F800

FASTA57362,180
        10         20         30         40         50         60 
MVKSTMSAVL LVLHIFVLHL QYSEVQSLAN TSSHDFSYLS FVYDATDPEL EGSYDYIIVG 

        70         80         90        100        110        120 
GGTAGCPLAA TLSANYSVLV LERGSLPTEY PNLLISDGFV YNLQQEDDGK TPVERFVSED 

       130        140        150        160        170        180 
GIDNVRGRVL GGTSMINAGV YVRANTSFFN QTGIEWDMDL VNQTYEWVED TIVFEPDSQT 

       190        200        210        220        230        240 
WQTVIGTAYL EAGILPNNGF SVDHLAGTRL TGSTFDNNGT RHASDELLNK GDPNNLRVAV 

       250        260        270        280        290        300 
QAAVEKIIFS SNTSGVTAIG VIYTDSNGTT HQAFVRGEGE VILSAGPIGS PQLLLLSGVG 

       310        320        330        340        350        360 
PESYLTSLNI SVVASHPYVG QYIYDNPRNF INILPPNPIE ASTVTVLGIT SDFYQCSISS 

       370        380        390        400        410        420 
LPFDTPPFSF FPTTSYPLPN QTFAHIVNKV PGPLSHGTVT LNSSSDVRVG PNVKFNYYSN 

       430        440        450        460        470        480 
LTDLSHCVSG MKKLGEVLST DALEPYKVED LPGIDGFNIL GIPLPENQTD DAAFETFCRE 

       490        500        510        520        530        540 
SVASYWHYHG GCLVGKVLDD GFRVTGINAL RVVDGSTFPS TPASHPQGFY LMLGRYMGIQ 

       550        560        570 
ILQERSASED AIRNLGFQEN ILDSPKSTSS FAF 

« Hide

References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51562 Genomic DNA. Translation: AAA96782.1.
AF013161 mRNA. Translation: AAB67714.1.
PIRT07948.

3D structure databases

ProteinModelPortalP52707.
SMRP52707. Positions 28-549.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR012132. 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.
PROSITEPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDL3_PRUSE
AccessionPrimary (citable) accession number: P52707
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 77 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