MDL4_PRUSE
ID MDL4_PRUSE Reviewed; 574 AA.
AC O82784;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=(R)-mandelonitrile lyase 4;
DE EC=4.1.2.10;
DE AltName: Full=Hydroxynitrile lyase 4;
DE Short=(R)-oxynitrilase 4;
DE Flags: Precursor;
GN Name=MDL4;
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 (MAR-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; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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; AF043186; AAD02265.1; -; mRNA.
DR EMBL; AF043187; AAD02266.1; -; Genomic_DNA.
DR EMBL; AF053884; AAC61980.1; -; mRNA.
DR EMBL; AF053885; AAC61981.1; -; Genomic_DNA.
DR PIR; T50766; T50766.
DR AlphaFoldDB; O82784; -.
DR SMR; O82784; -.
DR SABIO-RK; O82784; -.
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; 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..574
FT /note="(R)-mandelonitrile lyase 4"
FT /id="PRO_0000012343"
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 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 30
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 179
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 407
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 574 AA; 61682 MW; BCDFAE1DC5D2C539 CRC64;
MEKSTMSAVV LVLNLLVLHL QYSEVHSLAN TSSEHDFGYL KFVYNAVDLE LEGSYDYIIV
GGGTSGCPLA ATLSANYSVL VLERGTIATE YPNTLTVDGF AYNLQQQDDG KTPVERFVSE
DGIDNVRSRI LGGTTIINAG VYARANESFY NNSGVEWDLD LVNEAYEWVE DAIVYKPSNQ
SWQSITGTAF LEAGVHPDNG FGLVHEEGTR LTGSTFDNSG TRHASDELLN KGDPDNLKVA
VEAAVQKIIF STESSGLTAV GVVYTDSNGT SHRALVSGKG EVILSAGTLG TPQLLLLSGV
GPESYLTSLN ISVVASHPYV GQYVNDNPRN FINILPPNPI EPSTVTVLGI TSDFYQCSLS
SLPFDTPPFS LFPTTSYPLP NQTFAHIVSK VPGPLSAGSL TLQSSSNVSV APNVKFNYCS
DPVDLTHCVS GMKKIGVFLS TDALKPYKVD DLPGIDGFNI LGTPLPENQT DDAAFEKFCR
DTVASYWHYH GGAIVGKVID GNFRVTGINA LRVVDGSTFP ATPASHPQGF YLMLGRYVGT
KIVQERSASG EAIHTSTFKP KLMDSLKSAL SFAF
