ID T1K1W6_TETUR Unreviewed; 659 AA.
AC T1K1W6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN Name=107359373 {ECO:0000313|EnsemblMetazoa:tetur04g02900.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur04g02900.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur04g02900.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 EMBL; CAEY01001357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015781342.1; XM_015925856.1.
DR AlphaFoldDB; T1K1W6; -.
DR STRING; 32264.T1K1W6; -.
DR EnsemblMetazoa; tetur04g02900.1; tetur04g02900.1; tetur04g02900.
DR GeneID; 107359373; -.
DR KEGG; tut:107359373; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_7_0_1; -.
DR OMA; HIRIYPN; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000015104; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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 FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..659
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004580886"
FT DOMAIN 345..359
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 659 AA; 72677 MW; FF461C56242FD031 CRC64;
MVKIGAGFLL ICLTVIVQHN FVHTTSLPIN STAIRQSRIT NWLQRWNFNR FTELLPSFPD
LVSLISSVIG PIGLTSYSLT TVLPAVVKPD YDYIIVGGGT AGSVLANRLS EDGKSRVLLL
EAGVKEPDIN SIPFMNQLLR KTDTDWSYQS TPQLRSGLGL KGHQIPISRG KMIGGSSSQG
FMIYARGSPK DYDRWKSVGV NGWSFADVFP YFVKSEGASS LWDFEPGYHG LTGRLKVSQY
SSALNVETSI LGAIREAGWL IGDYNGKNQT TFAFSQFTID EGNRVSAGKA YLSDASSRPN
LDVCLESHVL RILFDDKKVA TGVEFKSSGN YYSVSVTKEI ILSAGAINTP QILMLSGIGP
KEHLEMHGIK VVVNAPGVGQ NLQDHPMTMI PFLTEKGSSF VYSRVFELFN NIYKYVIERK
GTLASPGTNI VGFYRTKYAD DRPDIQFQIE GTAFGGSYPT AFLGSLYNFR QELVDRYLAP
NTRLDGFTIY PILLHPKSKG SVKLASSNPL DPPLVDFNLY ENDRDIERLI EGCKQAVRIA
SMPSLIRINS RRFPGSPGLC GQYEFITDEY FKCYIQTITL TNNHPVGTVR MGSQDDKMSP
LDNKLKVKGV EKLRVVDASV IPEIVSGNLN GPIVMIAEKA ADIILDRPGL KAQSPPIKI
//