ID A0A200QK55_9MAGN Unreviewed; 563 AA.
AC A0A200QK55;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:OVA10777.1};
GN ORFNames=BVC80_8639g6 {ECO:0000313|EMBL:OVA10777.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA10777.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA10777.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA10777.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
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:OVA10777.1}.
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DR EMBL; MVGT01001846; OVA10777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QK55; -.
DR STRING; 56857.A0A200QK55; -.
DR InParanoid; A0A200QK55; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000195402; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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:SF2; (R)-MANDELONITRILE LYASE-LIKE; 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|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:UP000195402};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..563
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012826389"
FT DOMAIN 132..155
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 302..316
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 87..88
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 249
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 503..504
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 532
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 543..544
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 444..495
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 563 AA; 61982 MW; AA948C558B4B0B20 CRC64;
MAELKKPKEV LIPVLLSWIS LLLILILSLL FAQPSAQQQG PPYVQFIFNA TEFPFEDDYD
YIIVGGGTAG CPLAATLSQK YKVLLLERGG HNDEYPNLMT QEGFLSAITQ VDNYDSPAEA
FTSEDGVPNA RGRVLGGSSA INAGFYSRAD SEFYHLSGFD WDLDLVNRSY EWVEETVVFK
PDLKNWQSAI RDGLLEANVT PYNGFSLDHV SGTKIGGSTF DSSGRRHSAA DLLIKANFSN
LRVSLHASVE RILINSFSSD TPPIVSSGRA KQSAIGVVYR DQMGWRHNAM IRNQGEVILC
AGALGSPQLL LLSGIGPRPY LSSWGIPVAH HLPDVGHFMY DNPRNGISIV PPVPLDQSLI
QIVGITNSGS YIEAASNVVP FLSPPHSIFV HSPSTPIYLT VATLMEKIAG PLSVGWMRLA
STDVRVQPVV RFNYFSNPVD LARCVAGMRK IGEVLRGKSL EEFKSMEFFG RRDFRYVGPG
LPLNQSNDRL MAEFCRRTVS TIWHYHGGCV VGKVVDSQNR VIGVDGLRIV DGSTFSISPG
TNPQATLMML GRYINLYHYN LFL
//
