MDL2_PRUSE
ID MDL2_PRUSE Reviewed; 576 AA.
AC O50048;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=(R)-mandelonitrile lyase 2;
DE EC=4.1.2.10;
DE AltName: Full=Hydroxynitrile lyase 2;
DE Short=(R)-oxynitrilase 2;
DE Flags: Precursor;
GN Name=MDL2;
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].
RA Hu Z., Poulton J.E.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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; AF040078; AAB96763.1; -; mRNA.
DR EMBL; AF040079; AAB96764.1; -; Genomic_DNA.
DR PIR; T08073; T08073.
DR AlphaFoldDB; O50048; -.
DR SMR; O50048; -.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..576
FT /note="(R)-mandelonitrile lyase 2"
FT /id="PRO_0000012341"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 526
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 64..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 83..84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 138..141
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 487..488
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 527..528
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 428..479
FT /evidence="ECO:0000250"
SQ SEQUENCE 576 AA; 62724 MW; 570DC7853AE4D3EA CRC64;
MVKSTMSAIL VLALHLFVLH LQYSEVQSLA NTSAHDFSYL EFVYDANDTE LEGTYDYIIV
GGGTAGCPLA ATLSANYSVL VLERGTLPTE YPNLLTSDGF IYNLQQEDDG QTPVERFVSG
DGIDNVRGRV LGGTSMINAG VYVRANTSFF NQTGIEWDMD LVNKTYDWVE DTIVFKPDFQ
FWQNLTGTAF LEVGILPDNG FSLDHLEGTR LTGSTFDNNG TRHASDELLN KGDPNNLRVA
VHAAVEKIIF SSDSSGVTAI GVIYTDSNGT THQAFVRGDG EVILSAGPIG SPQLLLLSGV
GLESYLTSLN ISVVASHPYV GQYIYDNPRN FINILPPNPI EASTVTVLGI TSDFYQCSIS
SLPFSTAPFG FFPNPTYPLP NTTFAHIVNK VPGPLSHGTV LLQSTSDVRV APNVTFNYYS
NTTDLAHCVS GMKKIGEFLS SDALKPYKVE DLPGIEGFDI LGIPLPENQT DDAAFETFCR
EAVASYWHYH GGCLVGEVLD DDFRVTGINA LRVVDGSTFP STPASHPQGF YLMLGRYMGT
KILQERLASE EALHKSTFEP KILESLESAL SFAFES
