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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)DescriptionActionsGraphical viewLength
Binding sitei134FADBy similarity1
Binding sitei245FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei357SubstrateBy similarity1
Binding sitei486SubstrateBy similarity1
Active sitei488Proton donorBy similarity1
Binding sitei516FAD; via amide nitrogenBy similarity1
Active sitei526Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi64 – 65FADBy similarity2
Nucleotide bindingi83 – 84FADBy similarity2
Nucleotide bindingi138 – 141FADBy similarity4
Nucleotide bindingi487 – 488FADBy similarity2
Nucleotide bindingi527 – 528FADBy similarity2

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001234328 – 574(R)-mandelonitrile lyase 4Add BLAST547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi30N-linked (GlcNAc...)Sequence analysis1
Glycosylationi76N-linked (GlcNAc...)Sequence analysis1
Glycosylationi146N-linked (GlcNAc...)Sequence analysis1
Glycosylationi151N-linked (GlcNAc...)Sequence analysis1
Glycosylationi179N-linked (GlcNAc...)Sequence analysis1
Glycosylationi268N-linked (GlcNAc...)Sequence analysis1
Glycosylationi310N-linked (GlcNAc...)Sequence analysis1
Glycosylationi381N-linked (GlcNAc...)Sequence analysis1
Glycosylationi407N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi428 ↔ 479By similarity
Glycosylationi468N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO82784.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi294 – 297Poly-Leu4

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: October 5, 2016
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

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 one 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.