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Protein

(R)-mandelonitrile lyase 4

Gene

MDL4

Organism
Prunus serotina (Black cherry)
Status
Reviewed-Annotation score: Annotation score: 3 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

FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
(R)-mandelonitrile lyase 4 (EC:4.1.2.10)
Alternative name(s):
Hydroxynitrile lyase 4
Short name:
(R)-oxynitrilase 4
Gene namesi
Name:MDL4
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

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 574547(R)-mandelonitrile lyase 4PRO_0000012343Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi428 ↔ 479By similarity
Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO82784.
SMRiO82784. Positions 31-549.
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

InterProiIPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PROSITEiPS00624. GMC_OXRED_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O82784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSTMSAVV LVLNLLVLHL QYSEVHSLAN TSSEHDFGYL KFVYNAVDLE
60 70 80 90 100
LEGSYDYIIV GGGTSGCPLA ATLSANYSVL VLERGTIATE YPNTLTVDGF
110 120 130 140 150
AYNLQQQDDG KTPVERFVSE DGIDNVRSRI LGGTTIINAG VYARANESFY
160 170 180 190 200
NNSGVEWDLD LVNEAYEWVE DAIVYKPSNQ SWQSITGTAF LEAGVHPDNG
210 220 230 240 250
FGLVHEEGTR LTGSTFDNSG TRHASDELLN KGDPDNLKVA VEAAVQKIIF
260 270 280 290 300
STESSGLTAV GVVYTDSNGT SHRALVSGKG EVILSAGTLG TPQLLLLSGV
310 320 330 340 350
GPESYLTSLN ISVVASHPYV GQYVNDNPRN FINILPPNPI EPSTVTVLGI
360 370 380 390 400
TSDFYQCSLS SLPFDTPPFS LFPTTSYPLP NQTFAHIVSK VPGPLSAGSL
410 420 430 440 450
TLQSSSNVSV APNVKFNYCS DPVDLTHCVS GMKKIGVFLS TDALKPYKVD
460 470 480 490 500
DLPGIDGFNI LGTPLPENQT DDAAFEKFCR DTVASYWHYH GGAIVGKVID
510 520 530 540 550
GNFRVTGINA LRVVDGSTFP ATPASHPQGF YLMLGRYVGT KIVQERSASG
560 570
EAIHTSTFKP KLMDSLKSAL SFAF
Length:574
Mass (Da):61,682
Last modified:November 1, 1998 - v1
Checksum:iBCDFAE1DC5D2C539
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043186 mRNA. Translation: AAD02265.1.
AF043187 Genomic DNA. Translation: AAD02266.1.
AF053884 mRNA. Translation: AAC61980.1.
AF053885 Genomic DNA. Translation: AAC61981.1.
PIRiT50766.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043186 mRNA. Translation: AAD02265.1.
AF043187 Genomic DNA. Translation: AAD02266.1.
AF053884 mRNA. Translation: AAC61980.1.
AF053885 Genomic DNA. Translation: AAC61981.1.
PIRiT50766.

3D structure databases

ProteinModelPortaliO82784.
SMRiO82784. Positions 31-549.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PROSITEiPS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiMDL4_PRUSE
AccessioniPrimary (citable) accession number: O82784
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1998
Last modified: April 1, 2015
This is version 72 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.