P52706 (MDL1_PRUSE) 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 serotina (Black cherry)

Taxonomic identifier

23207 [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	563 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
Catalytic activity	(R)-mandelonitrile = cyanide + benzaldehyde.
Cofactor	FAD.
Subunit structure	Monomer.
Subcellular location	Vacuole › aleurone grain. Note: Primarily found within protein bodies of the cotyledonary parenchyma cells, with lesser amounts within the procambium.
Tissue specificity	Seeds. Localized within cotyledonary parenchyma cells. Ref.4
Developmental stage	Absent from maturing black cherry fruits until 6 weeks after flowering. Then, concomitant with cotyledon development, the level of enzyme increases with specificity for embryonal tissues. Ref.3 Ref.4
Post-translational modification	Glycosylated.
Sequence similarities	Belongs to the GMC oxidoreductase family.

Ontologies

Keywords
Cellular component	Vacuole
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Lyase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	alcohol metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	aleurone grain Inferred from electronic annotation. Source: UniProtKB-SubCell vacuole Inferred from electronic annotation. Source: UniProtKB-KW
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	Ref.3
	Chain	28 – 563	536	(R)-mandelonitrile lyase 1		PRO_0000012340
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	485 – 486	2	FAD By similarity
	Nucleotide binding	525 – 526	2	FAD By similarity
	Compositional bias	292 – 295	4	Poly-Leu
Sites
	Active site	486	1	Proton donor By similarity
	Active site	524	1	Proton acceptor By similarity
	Binding site	129	1	FAD; via carbonyl oxygen By similarity
	Binding site	133	1	FAD By similarity
	Binding site	244	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	355	1	Substrate By similarity
	Binding site	484	1	Substrate By similarity
	Binding site	514	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Glycosylation	145	1	N-linked (GlcNAc...) Potential
	Glycosylation	162	1	N-linked (GlcNAc...) Potential
	Glycosylation	379	1	N-linked (GlcNAc...) Potential
	Disulfide bond	426 ↔ 477		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52706 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 152367E736AF5FDD	FASTA	563	61,200
	10 20 30 40 50 60 MEKSTMSAIL LVLHLFVLLL QYSEVHSLAT TSNHDFSYLR FAYDATDLEL EGSYDYVIVG 70 80 90 100 110 120 GGTSGCPLAA TLSEKYKVLV LERGSLPTAY PNVLTADGFV YNLQQEDDGK TPVERFVSED 130 140 150 160 170 180 GIDNVRGRVL GGTSMINAGV YARANTSIYS ASGVDWDMDL VNKTYEWVED TIVFKPNYQP 190 200 210 220 230 240 WQSVTGTAFL EAGVDPNHGF SLDHEAGTRI TGSTFDNKGT RHAADELLNK GNSNNLRVGV 250 260 270 280 290 300 HASVEKIIFS NAPGLTATGV IYRDSNGTPH RAFVRSKGEV IVSAGTIGTP QLLLLSGVGP 310 320 330 340 350 360 ESYLSSLNIP VVLSHPYVGQ FLHDNPRNFI NILPPNPIEP TIVTVLGISN DFYQCSFSSL 370 380 390 400 410 420 PFTTPPFSFF PSTSYPLPNS TFAHFASKVA GPLSYGSLTL KSSSNVRVSP NVKFNYYSNP 430 440 450 460 470 480 TDLSHCVSGM KKIGELLSTD ALKPYKVEDL PGIEGFNILG IPLPKDQTDD AAFETFCRES 490 500 510 520 530 540 VASYWHYHGG CLVGKVLDGD FRVTGIDALR VVDGSTFPYT PASHPQGFYL MLGRYVGIKI 550 560 LQERSASDLK ILDSLKSAAS LVL

References

[1]	"Cloning of cDNA of Prunus serotina (R)-(+)-mandelonitrile lyase and identification of a putative FAD-binding site." Cheng I.-P., Poulton J.E. Plant Cell Physiol. 34:1139-1143(1993) Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Seed.
[2]	Hu Z., Poulton J.E. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Immunocytochemical localization of mandelonitrile lyase in mature black cherry (Prunus serotina Ehrh.) seeds." Wu H.-C., Poulton J.E. Plant Physiol. 96:1329-1337(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-43, DEVELOPMENTAL STAGE. Tissue: Seed.
[4]	"Temporal and spatial expression of amygdalin hydrolase and (R)-(+)-mandelonitrile lyase in black cherry seeds." Zheng L., Poulton J.E. Plant Physiol. 109:31-39(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X72617 mRNA. Translation: CAA51194.1. U78814 Genomic DNA. Translation: AAB38536.1.
PIR	S32156.
3D structure databases
ProteinModelPortal	P52706.
SMR	P52706. Positions 28-548.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	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.
PROSITE	PS00623. GMC_OXRED_1. 1 hit. PS00624. GMC_OXRED_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDL1_PRUSE

Accession

Primary (citable) accession number: P52706

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 9, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program