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Protein

(R)-mandelonitrile lyase 4

Gene

MDL4

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

Keywordsi

Molecular functionLyase
LigandFAD, 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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeAmygdaloideaeAmygdaleaePrunus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagineSequence analysis1
Glycosylationi76N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi146N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi151N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi179N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi268N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi310N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi381N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi407N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi428 ↔ 479By similarity
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO82784
SMRiO82784
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, 4 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR012132 GMC_OxRdtase
IPR000172 GMC_OxRdtase_N
IPR007867 GMC_OxRtase_C
PfamiView protein in Pfam
PF05199 GMC_oxred_C, 1 hit
PF00732 GMC_oxred_N, 1 hit
PIRSFiPIRSF000137 Alcohol_oxidase, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
PROSITEiView protein in PROSITE
PS00624 GMC_OXRED_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiMDL4_PRUSE
AccessioniPrimary (citable) accession number: O82784
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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