O24243 (MDL1_PRUDU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
(R)-mandelonitrile lyase 1
EC=4.1.2.10

Alternative name(s):
Hydroxynitrile lyase 1
Short name=(R)-oxynitrilase 1

Gene names

Name:

MDL1

Organism

Prunus dulcis (Almond) (Prunus amygdalus)

Taxonomic identifier

3755 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Rosaceae › Amygdaloideae › Amygdaleae › Prunus

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Catalytic activity	(R)-mandelonitrile = cyanide + benzaldehyde.
Cofactor	FAD By similarity.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Lyase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological_process	alcohol metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	choline dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro mandelonitrile lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	By similarity
	Chain	28 – 559	532	(R)-mandelonitrile lyase 1		PRO_0000012344
Regions
	Nucleotide binding	63 – 64	2	FAD By similarity
	Nucleotide binding	82 – 83	2	FAD By similarity
	Nucleotide binding	137 – 140	4	FAD By similarity
	Nucleotide binding	486 – 487	2	FAD By similarity
	Nucleotide binding	526 – 527	2	FAD By similarity
	Compositional bias	293 – 296	4	Poly-Leu
Sites
	Active site	487	1	Proton donor By similarity
	Active site	525	1	Proton acceptor By similarity
	Binding site	133	1	FAD By similarity
	Binding site	244	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	485	1	Substrate By similarity
Amino acid modifications
	Glycosylation	30	1	N-linked (GlcNAc...) Potential
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	145	1	N-linked (GlcNAc...) Potential
	Glycosylation	162	1	N-linked (GlcNAc...) Potential
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Glycosylation	218	1	N-linked (GlcNAc...) Potential
	Glycosylation	252	1	N-linked (GlcNAc...) Potential
	Glycosylation	255	1	N-linked (GlcNAc...) Potential
	Glycosylation	309	1	N-linked (GlcNAc...) Potential
	Glycosylation	380	1	N-linked (GlcNAc...) Potential
	Glycosylation	402	1	N-linked (GlcNAc...) Potential
	Glycosylation	420	1	N-linked (GlcNAc...) Potential
	Glycosylation	467	1	N-linked (GlcNAc...) Potential
	Disulfide bond	427 ↔ 478		By similarity

Sequences

	Sequence		Length	Mass (Da)
	O24243 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 58C2999EBF2E8A54	FASTA	559	61,100
	10 20 30 40 50 60 MEKSTMSVIL FVLHLLVLHL QYSEVHSLAN TSAHDFSYLK FVYNATDTSL EGSYDYIVIG 70 80 90 100 110 120 GGTSGCPLAA TLSEKYKVLL LERGTIATEY PNTLTADGFA YNLQQQDDGK TPVERFVSED 130 140 150 160 170 180 GIDNVRARIL GGTTIINAGV YARANISFYS QTGIEWDLDL VNKTYEWVED AIVVKPNNQS 190 200 210 220 230 240 WQSVIGEGFL EAGILPDNGF SLDHEAGTRL TGSTFDNNGT RHAADELLNK GDPNNLLVAV 250 260 270 280 290 300 QASVEKILFS SNTSNLSAIG VIYTDSDGNS HQAFVRGNGE VIVSAGTIGT PQLLLLSGVG 310 320 330 340 350 360 PESYLSSLNI TVVQPNPYVG QFLYNNPRNF INNFPPNPIE ASVVTVLGIR SDYYQVSLSS 370 380 390 400 410 420 LPFSTPPFSL FPTTSYPLPN STFAHIVSQV PGPLSHGSVT LNSSSDVRIA PNIKFNYYSN 430 440 450 460 470 480 STDLANCVSG MKKLGDLLRT KALEPYKARD VLGIDGFNYL GVPLPENQTD DASFETFCLD 490 500 510 520 530 540 NVASYWHYHG GSLVGKVLDD SFRVMGIKAL RVVDASTFPY EPNSHPQGFY LMLGRYVGLQ 550 ILQERSIRLE AIHNIQESM

References

[1]	Suelves M. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Texas. Tissue: Flower.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y08211 mRNA. Translation: CAA69388.1.
3D structure databases
ProteinModelPortal	O24243.
SMR	O24243. Positions 28-546.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001613. Flavin_amine_oxidase. IPR012132. GMC_OxRdtase. IPR000172. GMC_OxRdtase_N. IPR007867. GMC_OxRtase_C. [Graphical view]
Pfam	PF05199. GMC_oxred_C. 1 hit. PF00732. GMC_oxred_N. 1 hit. [Graphical view]
PIRSF	PIRSF000137. Alcohol_oxidase. 1 hit.
PRINTS	PR00757. AMINEOXDASEF.
PROSITE	PS00623. GMC_OXRED_1. 1 hit. PS00624. GMC_OXRED_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDL1_PRUDU

Accession

Primary (citable) accession number: O24243

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 28, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program