Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P52707

- MDL3_PRUSE

UniProt

P52707 - MDL3_PRUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

(R)-mandelonitrile lyase 3

Gene

MDL3

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.

Catalytic activityi

(R)-mandelonitrile = cyanide + benzaldehyde.

Cofactori

FAD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291FAD; via carbonyl oxygenBy similarity
Binding sitei133 – 1331FADBy similarity
Binding sitei244 – 2441FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei356 – 3561SubstrateBy similarity
Binding sitei485 – 4851SubstrateBy similarity
Active sitei487 – 4871Proton donorBy similarity
Binding sitei515 – 5151FAD; via amide nitrogenBy similarity
Active sitei525 – 5251Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi63 – 642FADBy similarity
Nucleotide bindingi82 – 832FADBy similarity
Nucleotide bindingi137 – 1404FADBy similarity
Nucleotide bindingi486 – 4872FADBy similarity
Nucleotide bindingi526 – 5272FADBy 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 3 (EC:4.1.2.10)
Alternative name(s):
Hydroxynitrile lyase 3
Short name:
(R)-oxynitrilase 3
Gene namesi
Name:MDL3
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 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 573546(R)-mandelonitrile lyase 3PRO_0000012342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi420 – 4201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi427 ↔ 478By similarity
Glycosylationi467 – 4671N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP52707.
SMRiP52707. Positions 28-549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi293 – 2964Poly-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.

P52707-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVKSTMSAVL LVLHIFVLHL QYSEVQSLAN TSSHDFSYLS FVYDATDPEL
60 70 80 90 100
EGSYDYIIVG GGTAGCPLAA TLSANYSVLV LERGSLPTEY PNLLISDGFV
110 120 130 140 150
YNLQQEDDGK TPVERFVSED GIDNVRGRVL GGTSMINAGV YVRANTSFFN
160 170 180 190 200
QTGIEWDMDL VNQTYEWVED TIVFEPDSQT WQTVIGTAYL EAGILPNNGF
210 220 230 240 250
SVDHLAGTRL TGSTFDNNGT RHASDELLNK GDPNNLRVAV QAAVEKIIFS
260 270 280 290 300
SNTSGVTAIG VIYTDSNGTT HQAFVRGEGE VILSAGPIGS PQLLLLSGVG
310 320 330 340 350
PESYLTSLNI SVVASHPYVG QYIYDNPRNF INILPPNPIE ASTVTVLGIT
360 370 380 390 400
SDFYQCSISS LPFDTPPFSF FPTTSYPLPN QTFAHIVNKV PGPLSHGTVT
410 420 430 440 450
LNSSSDVRVG PNVKFNYYSN LTDLSHCVSG MKKLGEVLST DALEPYKVED
460 470 480 490 500
LPGIDGFNIL GIPLPENQTD DAAFETFCRE SVASYWHYHG GCLVGKVLDD
510 520 530 540 550
GFRVTGINAL RVVDGSTFPS TPASHPQGFY LMLGRYMGIQ ILQERSASED
560 570
AIRNLGFQEN ILDSPKSTSS FAF
Length:573
Mass (Da):62,180
Last modified:October 1, 1996 - v1
Checksum:iDB181C68FED3F800
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U51562 Genomic DNA. Translation: AAA96782.1.
AF013161 mRNA. Translation: AAB67714.1.
PIRiT07948.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U51562 Genomic DNA. Translation: AAA96782.1 .
AF013161 mRNA. Translation: AAB67714.1 .
PIRi T07948.

3D structure databases

ProteinModelPortali P52707.
SMRi P52707. Positions 28-549.
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. "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].

Entry informationi

Entry nameiMDL3_PRUSE
AccessioniPrimary (citable) accession number: P52707
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3