ID A0A2P5APZ2_PARAD Unreviewed; 541 AA.
AC A0A2P5APZ2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=(R)-mandelonitrile lyase {ECO:0000256|ARBA:ARBA00013074};
DE EC=4.1.2.10 {ECO:0000256|ARBA:ARBA00013074};
GN ORFNames=PanWU01x14_311320 {ECO:0000313|EMBL:PON38626.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON38626.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
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:PON38626.1}.
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DR EMBL; JXTB01000490; PON38626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5APZ2; -.
DR STRING; 3476.A0A2P5APZ2; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000237105; 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:UP000237105};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..541
FT /note="(R)-mandelonitrile lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015185765"
FT DOMAIN 121..144
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 280..294
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 76..77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 127
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 238
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 481..482
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 510
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 521..522
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 422..473
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 541 AA; 58652 MW; F4EA8EC605BBAD4A CRC64;
MATALLSLSV LLLILLTNFH GQVLSLDHDF SYMKSVQNAS DLPLEAQYDY IVIGGGTAGC
PLAATLSEKY SVLVLERGGA PESYPNVLNV AGFFANLMEE DNGDTPAQRF TSEDGVDNLR
GRVLGGTSMI NAGFYSRADG EFLSESGIEW DSDEVEKAYE WVEETIVSRP SLAVWQSAVK
EALLDAGVVP DNGFTLNHEL GSKISGSTFD EVGRRHGSVE LLNKGDLKNL RVAVHATVER
LILSTKTSEP TATGVIYTDS KGKSHKALVH PKGEVILSAG TIGSPQLLLL SGIGPHSYLS
SLHIPIVHSQ PNVGKFMADN PRNNINLIIP FPIDPSSAQV VGITRDYFIE TVSYSLSFAP
NPSPFSLLPP QSSSDLSAAT IAEKIARPLS HGSLRLASTA EAKAAPHVRF NYFANPADLS
KCVSAMRKIG EMLETKSMDR FKYEDFRGSR GFLFLGPSLP TNQSDDSSME DFCRSSVTTF
WHYHGGCLLG KVVDENYRVM GTNSLRVVDG STFSTSPGTN PQATLMMLGR YIGLKMLRER
I
//
