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O50048

- MDL2_PRUSE

UniProt

O50048 - MDL2_PRUSE

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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

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.

Catalytic activityi

(R)-mandelonitrile = cyanide + benzaldehyde.

Cofactori

FAD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301FAD; via carbonyl oxygen By similarity
Binding sitei134 – 1341FAD By similarity
Binding sitei245 – 2451FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei357 – 3571Substrate By similarity
Binding sitei486 – 4861Substrate By similarity
Active sitei488 – 4881Proton donor By similarity
Binding sitei516 – 5161FAD; via amide nitrogen By similarity
Active sitei526 – 5261Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 652FAD By similarity
Nucleotide bindingi83 – 842FAD By similarity
Nucleotide bindingi138 – 1414FAD By similarity
Nucleotide bindingi487 – 4882FAD By similarity
Nucleotide bindingi527 – 5282FAD By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828 Reviewed predictionAdd
BLAST
Chaini29 – 576548(R)-mandelonitrile lyase 2PRO_0000012341Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliO50048.
SMRiO50048. Positions 29-550.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi294 – 2974Poly-Leu

Sequence similaritiesi

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: February 19, 2014
This is version 74 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

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