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O50048 (MDL2_PRUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 28, 2012. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
(R)-mandelonitrile lyase 2
EC=4.1.2.10
Alternative name(s):
Hydroxynitrile lyase 2
Short name=(R)-oxynitrilase 2
Gene names
Name:MDL2
OrganismPrunus serotina (Black cherry)
Taxonomic identifier23207 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Rosaceae › Amygdaloideae › Amygdaleae › Prunus

Protein attributes

Sequence length576 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.

Subunit structure

Monomer.

Subcellular location

Vacuole › aleurone 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 576548(R)-mandelonitrile lyase 2
PRO_0000012341

Regions

Nucleotide binding64 – 652FAD By similarity
Nucleotide binding83 – 842FAD By similarity
Nucleotide binding138 – 1414FAD By similarity
Nucleotide binding487 – 4882FAD By similarity
Nucleotide binding527 – 5282FAD By similarity
Compositional bias294 – 2974Poly-Leu

Sites

Active site4881Proton donor By similarity
Active site5261Proton acceptor By similarity
Binding site1301FAD; via carbonyl oxygen By similarity
Binding site1341FAD By similarity
Binding site2451FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site3571Substrate By similarity
Binding site4861Substrate By similarity
Binding site5161FAD; via amide nitrogen By similarity

Amino acid modifications

Glycosylation311N-linked (GlcNAc...) Potential
Glycosylation471N-linked (GlcNAc...) Potential
Glycosylation761N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation2681N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation4681N-linked (GlcNAc...) Potential
Disulfide bond428 ↔ 479 By similarity

Sequences

Sequence LengthMass (Da)Tools
O50048 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 570DC7853AE4D3EA

FASTA57662,724
        10         20         30         40         50         60 
MVKSTMSAIL VLALHLFVLH LQYSEVQSLA NTSAHDFSYL EFVYDANDTE LEGTYDYIIV 

        70         80         90        100        110        120 
GGGTAGCPLA ATLSANYSVL VLERGTLPTE YPNLLTSDGF IYNLQQEDDG QTPVERFVSG 

       130        140        150        160        170        180 
DGIDNVRGRV LGGTSMINAG VYVRANTSFF NQTGIEWDMD LVNKTYDWVE DTIVFKPDFQ 

       190        200        210        220        230        240 
FWQNLTGTAF LEVGILPDNG FSLDHLEGTR LTGSTFDNNG TRHASDELLN KGDPNNLRVA 

       250        260        270        280        290        300 
VHAAVEKIIF SSDSSGVTAI GVIYTDSNGT THQAFVRGDG EVILSAGPIG SPQLLLLSGV 

       310        320        330        340        350        360 
GLESYLTSLN ISVVASHPYV GQYIYDNPRN FINILPPNPI EASTVTVLGI TSDFYQCSIS 

       370        380        390        400        410        420 
SLPFSTAPFG FFPNPTYPLP NTTFAHIVNK VPGPLSHGTV LLQSTSDVRV APNVTFNYYS 

       430        440        450        460        470        480 
NTTDLAHCVS GMKKIGEFLS SDALKPYKVE DLPGIEGFDI LGIPLPENQT DDAAFETFCR 

       490        500        510        520        530        540 
EAVASYWHYH GGCLVGEVLD DDFRVTGINA LRVVDGSTFP STPASHPQGF YLMLGRYMGT 

       550        560        570 
KILQERLASE EALHKSTFEP KILESLESAL SFAFES

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF040078 mRNA. Translation: AAB96763.1.
AF040079 Genomic DNA. Translation: AAB96764.1.
PIRT08073.

3D structure databases

ProteinModelPortalO50048.
SMRO50048. Positions 29-550.
ModBaseSearch...

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 nameMDL2_PRUSE
AccessionPrimary (citable) accession number: O50048
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: November 28, 2012
This is version 71 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

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