MDL1_PRUDU
ID MDL1_PRUDU Reviewed; 559 AA.
AC O24243;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 dulcis (Almond) (Amygdalus dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3755;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Texas; TISSUE=Flower;
RA Suelves M.;
RL Submitted (SEP-1996) 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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; Y08211; CAA69388.1; -; mRNA.
DR PDB; 5EB4; X-ray; 2.30 A; A/B=28-559.
DR PDB; 5EB5; X-ray; 2.80 A; A/B=28-559.
DR PDB; 6JBY; X-ray; 1.60 A; A=26-559.
DR PDB; 6LQY; X-ray; 1.60 A; A=28-558.
DR PDB; 6LR8; X-ray; 1.59 A; A=28-558.
DR PDB; 7BWP; X-ray; 1.80 A; A=28-558.
DR PDB; 7CGS; X-ray; 1.60 A; A=28-558.
DR PDBsum; 5EB4; -.
DR PDBsum; 5EB5; -.
DR PDBsum; 6JBY; -.
DR PDBsum; 6LQY; -.
DR PDBsum; 6LR8; -.
DR PDBsum; 7BWP; -.
DR PDBsum; 7CGS; -.
DR AlphaFoldDB; O24243; -.
DR SMR; O24243; -.
DR BRENDA; 4.1.2.10; 5059.
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; IPR001613; Flavin_amine_oxidase.
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 PRINTS; PR00757; AMINEOXDASEF.
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 3D-structure; Disulfide bond; FAD; Flavoprotein; Glycoprotein; Lyase;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..559
FT /note="(R)-mandelonitrile lyase 1"
FT /id="PRO_0000012344"
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 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 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 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 44
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 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
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 255
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"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5EB4"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:6LR8"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:6LR8"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 270..283
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6LR8"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:5EB5"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 421..438
FT /evidence="ECO:0007829|PDB:6LR8"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 471..480
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:6LR8"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:7CGS"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:6LR8"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:6LR8"
FT HELIX 527..545
FT /evidence="ECO:0007829|PDB:6LR8"
SQ SEQUENCE 559 AA; 61100 MW; 58C2999EBF2E8A54 CRC64;
MEKSTMSVIL FVLHLLVLHL QYSEVHSLAN TSAHDFSYLK FVYNATDTSL EGSYDYIVIG
GGTSGCPLAA TLSEKYKVLL LERGTIATEY PNTLTADGFA YNLQQQDDGK TPVERFVSED
GIDNVRARIL GGTTIINAGV YARANISFYS QTGIEWDLDL VNKTYEWVED AIVVKPNNQS
WQSVIGEGFL EAGILPDNGF SLDHEAGTRL TGSTFDNNGT RHAADELLNK GDPNNLLVAV
QASVEKILFS SNTSNLSAIG VIYTDSDGNS HQAFVRGNGE VIVSAGTIGT PQLLLLSGVG
PESYLSSLNI TVVQPNPYVG QFLYNNPRNF INNFPPNPIE ASVVTVLGIR SDYYQVSLSS
LPFSTPPFSL FPTTSYPLPN STFAHIVSQV PGPLSHGSVT LNSSSDVRIA PNIKFNYYSN
STDLANCVSG MKKLGDLLRT KALEPYKARD VLGIDGFNYL GVPLPENQTD DASFETFCLD
NVASYWHYHG GSLVGKVLDD SFRVMGIKAL RVVDASTFPY EPNSHPQGFY LMLGRYVGLQ
ILQERSIRLE AIHNIQESM
