MDL3_PRUSE
ID MDL3_PRUSE Reviewed; 573 AA.
AC P52707;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=(R)-mandelonitrile lyase 3;
DE EC=4.1.2.10;
DE AltName: Full=Hydroxynitrile lyase 3;
DE Short=(R)-oxynitrilase 3;
DE Flags: Precursor;
GN Name=MDL3;
OS Prunus serotina (Black cherry).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=23207;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9414550; DOI=10.1104/pp.115.4.1359;
RA Hu Z., Poulton J.E.;
RT "Sequencing, genomic organization, and preliminary promoter analysis of a
RT black cherry (R)-(+)-mandelonitrile lyase gene.";
RL Plant Physiol. 115:1359-1369(1997).
CC -!- FUNCTION: Involved in cyanogenesis, the release of HCN from injured
CC tissues. Catalyzes the stereospecific addition of HCN to a variety of
CC aldehydes in vitro. It is a major seed constituent, and could have the
CC additional role of a storage form for reduced nitrogen.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mandelonitrile = benzaldehyde + hydrogen cyanide;
CC Xref=Rhea:RHEA:18313, ChEBI:CHEBI:17169, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:18450; EC=4.1.2.10;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain {ECO:0000250}.
CC Note=Primarily found within protein bodies of the cotyledonary
CC parenchyma cells, with lesser amounts within the procambium.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U51562; AAA96782.1; -; Genomic_DNA.
DR EMBL; AF013161; AAB67714.1; -; mRNA.
DR PIR; T07948; T07948.
DR AlphaFoldDB; P52707; -.
DR SMR; P52707; -.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046593; F:mandelonitrile lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Lyase; Signal; Vacuole.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..573
FT /note="(R)-mandelonitrile lyase 3"
FT /id="PRO_0000012342"
FT ACT_SITE 487
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 525
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 63..64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 82..83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 137..140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 486..487
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 526..527
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 427..478
FT /evidence="ECO:0000250"
SQ SEQUENCE 573 AA; 62180 MW; DB181C68FED3F800 CRC64;
MVKSTMSAVL LVLHIFVLHL QYSEVQSLAN TSSHDFSYLS FVYDATDPEL EGSYDYIIVG
GGTAGCPLAA TLSANYSVLV LERGSLPTEY PNLLISDGFV YNLQQEDDGK TPVERFVSED
GIDNVRGRVL GGTSMINAGV YVRANTSFFN QTGIEWDMDL VNQTYEWVED TIVFEPDSQT
WQTVIGTAYL EAGILPNNGF SVDHLAGTRL TGSTFDNNGT RHASDELLNK GDPNNLRVAV
QAAVEKIIFS SNTSGVTAIG VIYTDSNGTT HQAFVRGEGE VILSAGPIGS PQLLLLSGVG
PESYLTSLNI SVVASHPYVG QYIYDNPRNF INILPPNPIE ASTVTVLGIT SDFYQCSISS
LPFDTPPFSF FPTTSYPLPN QTFAHIVNKV PGPLSHGTVT LNSSSDVRVG PNVKFNYYSN
LTDLSHCVSG MKKLGEVLST DALEPYKVED LPGIDGFNIL GIPLPENQTD DAAFETFCRE
SVASYWHYHG GCLVGKVLDD GFRVTGINAL RVVDGSTFPS TPASHPQGFY LMLGRYMGIQ
ILQERSASED AIRNLGFQEN ILDSPKSTSS FAF
