ID M5XPX9_PRUPE Unreviewed; 550 AA.
AC M5XPX9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=(R)-mandelonitrile lyase {ECO:0000256|ARBA:ARBA00013074};
DE EC=4.1.2.10 {ECO:0000256|ARBA:ARBA00013074};
GN ORFNames=PRUPE_1G092400 {ECO:0000313|EMBL:ONI27529.1};
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI27529.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI27529.1, ECO:0000313|Proteomes:UP000006882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX PubMed=23525075; DOI=10.1038/ng.2586;
RA Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA Rokhsar D.S.;
RT "The high-quality draft genome of peach (Prunus persica) identifies unique
RT patterns of genetic diversity, domestication and genome evolution.";
RL Nat. Genet. 45:487-494(2013).
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 Evidence={ECO:0000256|ARBA:ARBA00001147};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; CM007651; ONI27529.1; -; Genomic_DNA.
DR RefSeq; XP_007226377.1; XM_007226315.1.
DR AlphaFoldDB; M5XPX9; -.
DR STRING; 3760.M5XPX9; -.
DR EnsemblPlants; ONI27529; ONI27529; PRUPE_1G092400.
DR GeneID; 18789360; -.
DR Gramene; ONI27529; ONI27529; PRUPE_1G092400.
DR KEGG; pper:18789360; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_026750_0_0_1; -.
DR OMA; NISGWTW; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000006882; Chromosome g1.
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; GMC_OXRDTASE_N 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; 2.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000137-3};
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 128..151
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 287..301
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 526
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 83..84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 138..141
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 245
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 487..488
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 516
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 527..528
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 428..479
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 550 AA; 59950 MW; BB31A5A4EA598527 CRC64;
MVKSTMSAIL VLVLHLFVLH LQYSEIHSLA NTSAHDFSYL EIVYDANDTE LEGTYDYIIV
GGGTAGCPLA ATLSANYSVL VLERGTLPTE YPNLLTSDGF IYNLQQEDDG QTPVERFVSG
DGIDNVRGRV LGGTSMINAG VYVRANTSFF NQTGIEWDMD LVNKTYDWVE DTIVFKPDFQ
FWQNLTRTAF LEVGILPDNG FSLDHIEGTR LTGSTFDNNG TRHASDELLN KGDPNNLRVA
VHAAVEKIIF SSNSSGVTAI GVIYTDSNGT THQAFVRGEG EVILSAGPIG SPQLLLLSGV
GPESYLTSLN ISVVASHPYV GQYIYDNPRN FINILPPNPI EPSTVTVLGI TSDFYQCSLS
SLPFSIAPFS FFPNPTYPLP KTTFAHIVNK VPGPLSYGTV TLQSTSDVRV APNVKFNYYS
NSTDLAHCVS GMKKIGEFLS SDALKPYKVE DLPGIEGFDI LGIPLPEDQT DDAAFETFCQ
VAVASYWHYH GGCLVGEVLD DDFRVTGINA LRVVDGSTFP STPASHPQGF YLMLGRYVGS
KILQERLASE
//