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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).By similarity

Catalytic activityi

(R)-mandelonitrile = cyanide + benzaldehyde.

Cofactori

FAD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301FAD; via carbonyl oxygenBy similarity
Binding sitei134 – 1341FADBy similarity
Binding sitei245 – 2451FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei357 – 3571SubstrateBy similarity
Binding sitei486 – 4861SubstrateBy similarity
Active sitei488 – 4881Proton donorBy similarity
Binding sitei516 – 5161FAD; via amide nitrogenBy similarity
Active sitei526 – 5261Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 652FADBy similarity
Nucleotide bindingi83 – 842FADBy similarity
Nucleotide bindingi138 – 1414FADBy similarity
Nucleotide bindingi487 – 4882FADBy similarity
Nucleotide bindingi527 – 5282FADBy 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. vacuole Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliO50048.
SMRiO50048. Positions 29-550.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

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

        10         20         30         40         50
MVKSTMSAIL VLALHLFVLH LQYSEVQSLA NTSAHDFSYL EFVYDANDTE
60 70 80 90 100
LEGTYDYIIV GGGTAGCPLA ATLSANYSVL VLERGTLPTE YPNLLTSDGF
110 120 130 140 150
IYNLQQEDDG QTPVERFVSG DGIDNVRGRV LGGTSMINAG VYVRANTSFF
160 170 180 190 200
NQTGIEWDMD LVNKTYDWVE DTIVFKPDFQ FWQNLTGTAF LEVGILPDNG
210 220 230 240 250
FSLDHLEGTR LTGSTFDNNG TRHASDELLN KGDPNNLRVA VHAAVEKIIF
260 270 280 290 300
SSDSSGVTAI GVIYTDSNGT THQAFVRGDG EVILSAGPIG SPQLLLLSGV
310 320 330 340 350
GLESYLTSLN ISVVASHPYV GQYIYDNPRN FINILPPNPI EASTVTVLGI
360 370 380 390 400
TSDFYQCSIS SLPFSTAPFG FFPNPTYPLP NTTFAHIVNK VPGPLSHGTV
410 420 430 440 450
LLQSTSDVRV APNVTFNYYS NTTDLAHCVS GMKKIGEFLS SDALKPYKVE
460 470 480 490 500
DLPGIEGFDI LGIPLPENQT DDAAFETFCR EAVASYWHYH GGCLVGEVLD
510 520 530 540 550
DDFRVTGINA LRVVDGSTFP STPASHPQGF YLMLGRYMGT KILQERLASE
560 570
EALHKSTFEP KILESLESAL SFAFES
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: October 29, 2014
This is version 76 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