Skip Header

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

(R)-mandelonitrile lyase 1

Gene

MDL1

Organism
Prunus dulcis (Almond) (Amygdalus dulcis)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Catalytic activityi

(R)-mandelonitrile = cyanide + benzaldehyde.

Cofactori

FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei133 – 1331FADBy similarity
Binding sitei244 – 2441FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei485 – 4851SubstrateBy similarity
Active sitei487 – 4871Proton donorBy 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

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi4.1.2.10. 5059.

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 dulcis (Almond) (Amygdalus dulcis)
Taxonomic identifieri3755 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Chaini28 – 559532(R)-mandelonitrile lyase 1PRO_0000012344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence analysis
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence analysis
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence analysis
Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence analysis
Glycosylationi255 – 2551N-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.By similarity

Structurei

Secondary structure

1
559
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 415Combined sources
Beta strandi42 – 443Combined sources
Helixi45 – 473Combined sources
Beta strandi50 – 5910Combined sources
Helixi65 – 728Combined sources
Turni73 – 753Combined sources
Beta strandi78 – 814Combined sources
Beta strandi83 – 853Combined sources
Helixi87 – 893Combined sources
Helixi91 – 944Combined sources
Helixi96 – 983Combined sources
Helixi99 – 1046Combined sources
Beta strandi109 – 1179Combined sources
Beta strandi123 – 1275Combined sources
Helixi132 – 1354Combined sources
Helixi147 – 1526Combined sources
Helixi158 – 17215Combined sources
Helixi180 – 19112Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi206 – 2105Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi219 – 2213Combined sources
Helixi224 – 2307Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2416Combined sources
Beta strandi243 – 2497Combined sources
Beta strandi257 – 2648Combined sources
Beta strandi270 – 28314Combined sources
Helixi286 – 29611Combined sources
Helixi302 – 3076Combined sources
Beta strandi313 – 3153Combined sources
Turni317 – 3204Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi327 – 3348Combined sources
Beta strandi346 – 3505Combined sources
Beta strandi353 – 3608Combined sources
Beta strandi371 – 3744Combined sources
Beta strandi383 – 3897Combined sources
Beta strandi397 – 4004Combined sources
Beta strandi402 – 4054Combined sources
Beta strandi407 – 4093Combined sources
Beta strandi412 – 4143Combined sources
Helixi421 – 43818Combined sources
Turni441 – 4433Combined sources
Helixi444 – 4463Combined sources
Helixi454 – 4563Combined sources
Beta strandi457 – 4615Combined sources
Helixi471 – 48111Combined sources
Beta strandi489 – 4924Combined sources
Turni495 – 4973Combined sources
Beta strandi502 – 5043Combined sources
Beta strandi510 – 5123Combined sources
Helixi515 – 5173Combined sources
Beta strandi522 – 5254Combined sources
Helixi527 – 54519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5EB4X-ray2.30A/B28-559[»]
5EB5X-ray2.80A/B28-559[»]
ProteinModelPortaliO24243.
SMRiO24243. Positions 28-546.
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

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 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.

O24243-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKSTMSVIL FVLHLLVLHL QYSEVHSLAN TSAHDFSYLK FVYNATDTSL
60 70 80 90 100
EGSYDYIVIG GGTSGCPLAA TLSEKYKVLL LERGTIATEY PNTLTADGFA
110 120 130 140 150
YNLQQQDDGK TPVERFVSED GIDNVRARIL GGTTIINAGV YARANISFYS
160 170 180 190 200
QTGIEWDLDL VNKTYEWVED AIVVKPNNQS WQSVIGEGFL EAGILPDNGF
210 220 230 240 250
SLDHEAGTRL TGSTFDNNGT RHAADELLNK GDPNNLLVAV QASVEKILFS
260 270 280 290 300
SNTSNLSAIG VIYTDSDGNS HQAFVRGNGE VIVSAGTIGT PQLLLLSGVG
310 320 330 340 350
PESYLSSLNI TVVQPNPYVG QFLYNNPRNF INNFPPNPIE ASVVTVLGIR
360 370 380 390 400
SDYYQVSLSS LPFSTPPFSL FPTTSYPLPN STFAHIVSQV PGPLSHGSVT
410 420 430 440 450
LNSSSDVRIA PNIKFNYYSN STDLANCVSG MKKLGDLLRT KALEPYKARD
460 470 480 490 500
VLGIDGFNYL GVPLPENQTD DASFETFCLD NVASYWHYHG GSLVGKVLDD
510 520 530 540 550
SFRVMGIKAL RVVDASTFPY EPNSHPQGFY LMLGRYVGLQ ILQERSIRLE

AIHNIQESM
Length:559
Mass (Da):61,100
Last modified:January 1, 1998 - v1
Checksum:i58C2999EBF2E8A54
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08211 mRNA. Translation: CAA69388.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y08211 mRNA. Translation: CAA69388.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5EB4X-ray2.30A/B28-559[»]
5EB5X-ray2.80A/B28-559[»]
ProteinModelPortaliO24243.
SMRiO24243. Positions 28-546.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.1.2.10. 5059.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMDL1_PRUDU
AccessioniPrimary (citable) accession number: O24243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: September 7, 2016
This is version 81 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.