ID A0A3Q7GVK8_SOLLC Unreviewed; 597 AA.
AC A0A3Q7GVK8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN Name=101264132 {ECO:0000313|EnsemblPlants:Solyc06g062600.3.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc06g062600.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc06g062600.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc06g062600.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc06g062600.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc06g062600.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
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 RefSeq; XP_004241869.1; XM_004241821.3.
DR AlphaFoldDB; A0A3Q7GVK8; -.
DR STRING; 4081.A0A3Q7GVK8; -.
DR PaxDb; 4081-Solyc06g062600-2-1; -.
DR EnsemblPlants; Solyc06g062600.3.1; Solyc06g062600.3.1; Solyc06g062600.3.
DR GeneID; 101264132; -.
DR Gramene; Solyc06g062600.3.1; Solyc06g062600.3.1; Solyc06g062600.3.
DR KEGG; sly:101264132; -.
DR InParanoid; A0A3Q7GVK8; -.
DR OMA; NYPWIHI; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000004994; Chromosome 6.
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; OSJNBA0019K04.7 PROTEIN; 1.
DR PANTHER; PTHR45968:SF17; PROTEIN HOTHEAD-LIKE ISOFORM X1; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
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:UP000004994};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..597
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018591272"
FT DOMAIN 297..311
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 94..95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 140
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 253
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 531..532
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 560
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 571..572
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT DISULFID 467..523
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-3"
SQ SEQUENCE 597 AA; 65436 MW; A1CE81DEBAB46F7F CRC64;
MAVVIGAVMP VIVKLLLLLL CLNFNSSLTQ ARKWESWKDK YPFIKPASSF SSSNAWSSGS
SKGHNYDYII VGGGTAGCPL AATLSQKFNV LLLERGGVPF ANANVSLMQN FHISLADTSP
HSASQIFAST DGVFNARARV LGGGTCINAG FYSRASQSYI KKAGWDSKLV NESFPWIEKQ
IVHKPILAPW QKAVSDGLLE VGISPYNGFT YDHIYGTKFG GTLFDRFGHR KTAADLLTSA
NPEKLDVLVH AMVQKIEFDT SGRKPRAVGV IFKDEKGNQH TAFLSKRKGS EIIVSSGAIG
SPQILLLSGI GPKAELKKLN ISVVFDNKFV GKGMSDNPLN TIFVPTNRPV QQSLIQTVGI
TKMGVYIEAS SGYGETEDSI HCHHGIVSAE IGQLSAIPPK QRTLEAIEVY KRNKKHVPQE
AFRGGFILEK IATPLSTGHI SLKSTKVDDS PSVTFNYFSH PRDLKRCVDG IRIVEQIVKS
KHFTTYAQCD KDTLDKLLNM SVQANINLIP KHTNDTESLE QFCKDTVTTI WHYHGGCQVG
KVVTPDYRVM NVNRLRVIDG STFNESPGTN PQATVLMMGR YMGVKILRER LGRAAGL
//
