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P52706

- MDL1_PRUSE

UniProt

P52706 - MDL1_PRUSE

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Protein
(R)-mandelonitrile lyase 1
Gene
MDL1
Organism
Prunus serotina (Black cherry)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.

Catalytic activityi

(R)-mandelonitrile = cyanide + benzaldehyde.

Cofactori

FAD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291FAD; via carbonyl oxygen By similarity
Binding sitei133 – 1331FAD By similarity
Binding sitei244 – 2441FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei355 – 3551Substrate By similarity
Binding sitei484 – 4841Substrate By similarity
Active sitei486 – 4861Proton donor By similarity
Binding sitei514 – 5141FAD; via amide nitrogen By similarity
Active sitei524 – 5241Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi63 – 642FAD By similarity
Nucleotide bindingi82 – 832FAD By similarity
Nucleotide bindingi137 – 1404FAD By similarity
Nucleotide bindingi485 – 4862FAD By similarity
Nucleotide bindingi525 – 5262FAD 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 1 (EC:4.1.2.10)
Alternative name(s):
Hydroxynitrile lyase 1
Short name:
(R)-oxynitrilase 1
Gene namesi
Name:MDL1
OrganismiPrunus serotina (Black cherry)
Taxonomic identifieri23207 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

Subcellular locationi

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

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 – 27271 Publication
Add
BLAST
Chaini28 – 563536(R)-mandelonitrile lyase 1
PRO_0000012340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi145 – 1451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi162 – 1621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi379 – 3791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi426 ↔ 477 By similarity

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Seeds. Localized within cotyledonary parenchyma cells.1 Publication

Developmental stagei

Absent from maturing black cherry fruits until 6 weeks after flowering. Then, concomitant with cotyledon development, the level of enzyme increases with specificity for embryonal tissues.2 Publications

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP52706.
SMRiP52706. Positions 28-548.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi292 – 2954Poly-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.

P52706-1 [UniParc]FASTAAdd to Basket

« Hide

MEKSTMSAIL LVLHLFVLLL QYSEVHSLAT TSNHDFSYLR FAYDATDLEL    50
EGSYDYVIVG GGTSGCPLAA TLSEKYKVLV LERGSLPTAY PNVLTADGFV 100
YNLQQEDDGK TPVERFVSED GIDNVRGRVL GGTSMINAGV YARANTSIYS 150
ASGVDWDMDL VNKTYEWVED TIVFKPNYQP WQSVTGTAFL EAGVDPNHGF 200
SLDHEAGTRI TGSTFDNKGT RHAADELLNK GNSNNLRVGV HASVEKIIFS 250
NAPGLTATGV IYRDSNGTPH RAFVRSKGEV IVSAGTIGTP QLLLLSGVGP 300
ESYLSSLNIP VVLSHPYVGQ FLHDNPRNFI NILPPNPIEP TIVTVLGISN 350
DFYQCSFSSL PFTTPPFSFF PSTSYPLPNS TFAHFASKVA GPLSYGSLTL 400
KSSSNVRVSP NVKFNYYSNP TDLSHCVSGM KKIGELLSTD ALKPYKVEDL 450
PGIEGFNILG IPLPKDQTDD AAFETFCRES VASYWHYHGG CLVGKVLDGD 500
FRVTGIDALR VVDGSTFPYT PASHPQGFYL MLGRYVGIKI LQERSASDLK 550
ILDSLKSAAS LVL 563
Length:563
Mass (Da):61,200
Last modified:October 1, 1996 - v1
Checksum:i152367E736AF5FDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X72617 mRNA. Translation: CAA51194.1.
U78814 Genomic DNA. Translation: AAB38536.1.
PIRiS32156.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X72617 mRNA. Translation: CAA51194.1 .
U78814 Genomic DNA. Translation: AAB38536.1 .
PIRi S32156.

3D structure databases

ProteinModelPortali P52706.
SMRi P52706. Positions 28-548.
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. "Cloning of cDNA of Prunus serotina (R)-(+)-mandelonitrile lyase and identification of a putative FAD-binding site."
    Cheng I.-P., Poulton J.E.
    Plant Cell Physiol. 34:1139-1143(1993)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Seed.
  2. Hu Z., Poulton J.E.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Immunocytochemical localization of mandelonitrile lyase in mature black cherry (Prunus serotina Ehrh.) seeds."
    Wu H.-C., Poulton J.E.
    Plant Physiol. 96:1329-1337(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-43, DEVELOPMENTAL STAGE.
    Tissue: Seed.
  4. "Temporal and spatial expression of amygdalin hydrolase and (R)-(+)-mandelonitrile lyase in black cherry seeds."
    Zheng L., Poulton J.E.
    Plant Physiol. 109:31-39(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMDL1_PRUSE
AccessioniPrimary (citable) accession number: P52706
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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