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   27-MAR-2024, entry version 107.
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   GlyCosmos; P52707; 13 sites, No reported glycans.
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; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   PANTHER; PTHR45968:SF23; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45968; OSJNBA0019K04.7 PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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
//