ID A0A232EXM1_9HYME Unreviewed; 590 AA.
AC A0A232EXM1;
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:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=TSAR_011602 {ECO:0000313|EMBL:OXU23050.1};
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:OXU23050.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU23050.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU23050.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU23050.1};
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 -!- 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:OXU23050.1}.
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DR EMBL; NNAY01001745; OXU23050.1; -; Genomic_DNA.
DR STRING; 543379.A0A232EXM1; -.
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; 2.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
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:SF227; GLUCOSE DEHYDROGENASE [FAD, QUINONE]-LIKE PROTEIN; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 2.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000215335}.
FT DOMAIN 2..139
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 241..319
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 432..575
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 520
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 564
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OXU23050.1"
SQ SEQUENCE 590 AA; 65770 MW; FA20344DB97A04DB CRC64;
GFLKAGIELG YPVVDYNAYN QSVGFSYIQS TMKNGIRMST NRAYLYPANN RKNLFVTKLS
HVDRILINPE TKRAYGVEFT KFGKKIRAMA RKEIILSAGV VGSAQLLMLS GIGPSKHLKE
MKIDVVQDAP VGENLMDHIA YGGLVFLLDQ PIGILTKDMV NFAKPYLSDY LIRKTGPFTI
PGGCEALAFI DVDKPTKLDV YPNIELLFIG ASIVSDSVIH XDEHEQSLSV SREQQEEPLS
HVDRILINPE TKRAYGVEFT KLGKKIRAIA RKEIILSAGA VGSAQLLMLS GIGPSKHLKE
MKIDVVQDAP VGENLMDHIA YGGLVFLVDQ PVGIVTEDMV NFAKPYLTDY LIRKTGPFTI
PGGCEALAFI DVDKPTKLDV FPNIELLFIG ASIVSDSVIH KNMGISNKYW NQMYSNISGH
YSWTIFPMLM RPKSRGKILL RSNDPNEKPK IFAGYLQDPE DVRIMVKGIR SALEVSRTRA
MRKFKSQFHE VPVPGCEHRQ YDSDEYWECA LRTFTITIYH QSGTCKMAPD NDPTGVVNPR
LQVKGIQGLR VADASIMPMI VTGHTNIPVI MIGEKLADIV KEDWGYKVEV
//
