ID A0A232FF98_9HYME Unreviewed; 598 AA.
AC A0A232FF98;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=TSAR_016232 {ECO:0000313|EMBL:OXU29434.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU29434.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU29434.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU29434.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU29434.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(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}.
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:OXU29434.1}.
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DR EMBL; NNAY01000290; OXU29434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232FF98; -.
DR STRING; 543379.A0A232FF98; -.
DR Proteomes; UP000215335; 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:SF154; FI04917P; 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|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335}.
FT DOMAIN 311..325
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 598 AA; 66328 MW; 6A26E5A5314894C2 CRC64;
MTWAPANCSG SCTSQVLNFF TFLVQYLGFS YDSKFTSTKT DEKESGLRDE FDFIVVGAGS
AGCVVANRLS EIEEWKVLLL ESGDEEPAVT GVPGLWPVLR SSSLDYGYYT EPEPAICAAA
ANKSCHVVRG KVMGGTSALN DMIYARGNKQ DYNDWENLGN AGWGFEDVLP YFKKSEDARD
PLLLAKNPDS HGTGGYLTTE QFPYKNKNGR AIIDAWKELG LEEVDYNSGS QIGVSNLQFN
SIHGSRLSAN GAFIRPIRGR RSNLVVRPNS RVTRVMINRY SKRVMGVEYF CSKTSTLKMV
YAKKEVIISA GAFDSPKLLM LSGVGPAEHL REAGIWVVKN SPVGRNLHEH TVIVPFTFDL
KKESRTTSSF DDMRNDLVYW MSSHEGVLSS TGLQSTVAFL QTSFESRPGV PDIQVGFAGS
STSSDSASIA TSYYDKAVIF LVLLKPHSRG HLRLNVSDPL WSQPLIQLNS MTDPRDSEIL
VEGVKLASKV TRTKSLKQKG FIRTKPAMCQ EYEVDSREYF ECFVKRYTFT SYHPVGTCKM
GPKRDKDAVV DPRLRVYGVT GLRVIDASIM PQTTRGSINA PIIMIGEKGS DMIKEDWL
//
