ID W1PRP9_AMBTC Unreviewed; 542 AA.
AC W1PRP9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=AMTR_s00025p00245990 {ECO:0000313|EMBL:ERN12677.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN12677.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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}.
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DR EMBL; KI392614; ERN12677.1; -; Genomic_DNA.
DR AlphaFoldDB; W1PRP9; -.
DR STRING; 13333.W1PRP9; -.
DR EnsemblPlants; ERN12677; ERN12677; AMTR_s00025p00245990.
DR Gramene; ERN12677; ERN12677; AMTR_s00025p00245990.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_026750_0_0_1; -.
DR OMA; PVPNCKH; -.
DR Proteomes; UP000017836; 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; 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};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 270..284
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 81..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 472..473
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 501
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 512..513
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 411..464
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 542 AA; 59290 MW; E0F2E04811E25CF7 CRC64;
MHSSKGGGRT KPLYVQLALN ATEFPAEDEY DYIVVGGGTA GCPLAATLSA NPNSLRVLLL
ERGSDPLSYP ALSSPRGFFS TLNEDNSPDS PAQRFESEDG VPNARGRVLG GSSAINAGFY
TRAEPDFFAP GKPGYWDMGL VNRSYQWVER AVLFQPRLTT WQADFRDALL EANVTPFNGF
RLDHVEGTKI GGSTFDGTRR RHSAADLLNY ARPENIHVAL HATVEKVLFT SVQGTGVPRP
TAIGVVYADL QGRPHHAMLL PRGEVILSAG AIGSPQLLML SGIGSNRSLI RWGIPVAHHL
PAVGNTMRDN PRNALSFVSP VRLPLSLIQV VAITPNVFLE AASNLLPFSP RSRSLFLSPR
YSSIPLNIAS LMAKIPGPLS SGSLRLASSN VRDNPLVRFN YFDEGLDLQR CMEGVRLVAR
VLGTSAMDQF KFPGRHFGER EFWYLDDVRL PANLSNDDAV AEFCHRTVST IWHYHGGCVM
GEVVDTQYRV FGVQALRVVD GSTFSHSPGT NPQATVMMLG RYVGVKMLEE RRASDRDTKI
RA
//
