MDL1_PRUSE
ID MDL1_PRUSE Reviewed; 563 AA.
AC P52706;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=(R)-mandelonitrile lyase 1;
DE EC=4.1.2.10;
DE AltName: Full=Hydroxynitrile lyase 1;
DE Short=(R)-oxynitrilase 1;
DE Flags: Precursor;
GN Name=MDL1;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Seed;
RA Cheng I.-P., Poulton J.E.;
RT "Cloning of cDNA of Prunus serotina (R)-(+)-mandelonitrile lyase and
RT identification of a putative FAD-binding site.";
RL Plant Cell Physiol. 34:1139-1143(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hu Z., Poulton J.E.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 28-43, AND DEVELOPMENTAL STAGE.
RC TISSUE=Seed;
RX PubMed=16668338; DOI=10.1104/pp.96.4.1329;
RA Wu H.-C., Poulton J.E.;
RT "Immunocytochemical localization of mandelonitrile lyase in mature black
RT cherry (Prunus serotina Ehrh.) seeds.";
RL Plant Physiol. 96:1329-1337(1991).
RN [4]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=7480328; DOI=10.1104/pp.109.1.31;
RA Zheng L., Poulton J.E.;
RT "Temporal and spatial expression of amygdalin hydrolase and (R)-(+)-
RT mandelonitrile lyase in black cherry seeds.";
RL Plant Physiol. 109:31-39(1995).
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. Note=Primarily found
CC within protein bodies of the cotyledonary parenchyma cells, with lesser
CC amounts within the procambium.
CC -!- TISSUE SPECIFICITY: Seeds. Localized within cotyledonary parenchyma
CC cells. {ECO:0000269|PubMed:7480328}.
CC -!- DEVELOPMENTAL STAGE: Absent from maturing black cherry fruits until 6
CC weeks after flowering. Then, concomitant with cotyledon development,
CC the level of enzyme increases with specificity for embryonal tissues.
CC {ECO:0000269|PubMed:16668338, ECO:0000269|PubMed:7480328}.
CC -!- PTM: Glycosylated.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X72617; CAA51194.1; -; mRNA.
DR EMBL; U78814; AAB38536.1; -; Genomic_DNA.
DR PIR; S32156; S32156.
DR AlphaFoldDB; P52706; -.
DR SMR; P52706; -.
DR BRENDA; 4.1.2.10; 5069.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein; Glycoprotein;
KW Lyase; Signal; Vacuole.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:16668338"
FT CHAIN 28..563
FT /note="(R)-mandelonitrile lyase 1"
FT /id="PRO_0000012340"
FT ACT_SITE 486
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 524
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 355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 485..486
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 514
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 525..526
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 145
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 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 426..477
FT /evidence="ECO:0000250"
SQ SEQUENCE 563 AA; 61200 MW; 152367E736AF5FDD CRC64;
MEKSTMSAIL LVLHLFVLLL QYSEVHSLAT TSNHDFSYLR FAYDATDLEL EGSYDYVIVG
GGTSGCPLAA TLSEKYKVLV LERGSLPTAY PNVLTADGFV YNLQQEDDGK TPVERFVSED
GIDNVRGRVL GGTSMINAGV YARANTSIYS ASGVDWDMDL VNKTYEWVED TIVFKPNYQP
WQSVTGTAFL EAGVDPNHGF SLDHEAGTRI TGSTFDNKGT RHAADELLNK GNSNNLRVGV
HASVEKIIFS NAPGLTATGV IYRDSNGTPH RAFVRSKGEV IVSAGTIGTP QLLLLSGVGP
ESYLSSLNIP VVLSHPYVGQ FLHDNPRNFI NILPPNPIEP TIVTVLGISN DFYQCSFSSL
PFTTPPFSFF PSTSYPLPNS TFAHFASKVA GPLSYGSLTL KSSSNVRVSP NVKFNYYSNP
TDLSHCVSGM KKIGELLSTD ALKPYKVEDL PGIEGFNILG IPLPKDQTDD AAFETFCRES
VASYWHYHGG CLVGKVLDGD FRVTGIDALR VVDGSTFPYT PASHPQGFYL MLGRYVGIKI
LQERSASDLK ILDSLKSAAS LVL
