ID A0A022QCR2_ERYGU Unreviewed; 556 AA.
AC A0A022QCR2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MIMGU_mgv1a003898mg {ECO:0000313|EMBL:EYU25043.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU25043.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU25043.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KI632098; EYU25043.1; -; Genomic_DNA.
DR RefSeq; XP_012851974.1; XM_012996520.1.
DR AlphaFoldDB; A0A022QCR2; -.
DR STRING; 4155.A0A022QCR2; -.
DR GeneID; 105971657; -.
DR KEGG; egt:105971657; -.
DR eggNOG; KOG1238; Eukaryota.
DR OMA; INYMIYI; -.
DR OrthoDB; 52047at2759; -.
DR PhylomeDB; A0A022QCR2; -.
DR Proteomes; UP000030748; 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:SF31; GLUCOSE-METHANOL-CHOLINE (GMC) OXIDOREDUCTASE FAMILY 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.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000137-3};
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 50..323
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 398..543
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 78..79
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 494..495
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 523
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 534..535
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 431..486
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 556 AA; 61332 MW; 2C67D9706CB26DDE CRC64;
MASVITYRWS PLLAVSLWIF FFIIIACYAE KAPYSSFARD ATSAPPSEYF DYIIVGGGTA
GCALAATLSA SAKVLLLERG GLPYGDPNLG HVTGFRKTLA DTSTTSPSQL FVSTDGVFNH
RGRVLGGSSA INAGFYTRAS NQYVVEAGWD PRLVNESYGW VETKVVFRPR VLEWQSAVRD
GLLEAGVSPL RGTTYEHLHG TKTGGSTFDE HGYRHTAADL LEYADPAKIT VYLYATVYKI
LFGSSPERRT KSYGVLFRDS KGNRHVAYLN SGPTNEVILS AGALGSPQLL MLNGIGPARQ
LRAHGITVIL DQPMVGQGMS DNPMNAVIIP SHRPVEVSLI QVVGITNAGS YIEAASRVLE
QALTPALVQH FTRLANQTFP EGTRNIQDVI ILEKVMGPFS RGYLELQSND PNDNPRVTFN
YFQDPRDLQR CVQGMGIVKR VIESRPVSAF RYPFSTFQSL INLMLAIPNN LRRRHVSASH
SMEQFCVDTV MTIWHYHGGC QVDRVVDRDY RVIGVDGLRV IDGSTFYTSP GTNPQATVMM
LGRYMGQKIL RERIPQ
//
