ID A0A2P5E1G4_TREOI Unreviewed; 548 AA.
AC A0A2P5E1G4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=(R)-mandelonitrile lyase {ECO:0000256|ARBA:ARBA00013074};
DE EC=4.1.2.10 {ECO:0000256|ARBA:ARBA00013074};
GN ORFNames=TorRG33x02_236290 {ECO:0000313|EMBL:PON79347.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON79347.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PON79347.1}.
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DR EMBL; JXTC01000236; PON79347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5E1G4; -.
DR STRING; 63057.A0A2P5E1G4; -.
DR InParanoid; A0A2P5E1G4; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000237000; Unassembled WGS sequence.
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; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL 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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..548
FT /note="(R)-mandelonitrile lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015173187"
FT DOMAIN 124..147
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 283..297
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 79..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 126
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 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 485..486
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 514
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 525..526
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 426..477
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 548 AA; 59548 MW; 633A12790C3913E9 CRC64;
MGPAPLHSLL IIFAIFSISF DSRVHVLASD YDFSYMKSVR NATDLPLEEE YDYIVIGGGT
AGCPLAATLS QNHSVLVLER GNVPKAHPNV LHASGFLANL IEEDNGDNPA QKFTSEDGVE
NARGRVLGGT SMINAGFFSR ADSEFLSKSG IQWDLDAVEK AYEWVEETIV SFPNLSVWQS
DAKEALLEAG LGPDNGVTTK HVLGTKVSGS TFDEEGRRHG AVELLNKGNL KNLVVAIHAT
VKRIIFSTKT SNPSAIGVIY TDSRGRPHKA LIRQKGEIIS SAGALGSPQL LLLSGIGPHS
YLSSLHIPVV HSQPNVGKFM ADNPRNNINL IIPFPFDPST ARVVGITSDY YIETVSYSLQ
FSPTFLPFGF YPTPLSPANL SLASIVEKIV GPLSHGSLHL ASPTDVKATP HVRFNYFTDP
IDLSRCVNAT RKLGELLKTK SLDRFKYQDL NGVRDYFFLG PPLPTNYSDV SSIEAFCRST
VTTIWHYHGG SLVGKVVDGD YKVIGINSLR VVDGSTFTLS PGTNPQATLM MIGRYVGLKI
LRERGDPN
//
