ID A0A0L7R773_9HYME Unreviewed; 607 AA.
AC A0A0L7R773;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE SubName: Full=Glucose dehydrogenase [acceptor] {ECO:0000313|EMBL:KOC66688.1};
DE Flags: Fragment;
GN ORFNames=WH47_00897 {ECO:0000313|EMBL:KOC66688.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC66688.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC66688.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC66688.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ414643; KOC66688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7R773; -.
DR SMR; A0A0L7R773; -.
DR STRING; 597456.A0A0L7R773; -.
DR EnsemblMetazoa; XM_017933142.1; XP_017788631.1; LOC108571159.
DR Proteomes; UP000053825; 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:SF217; GLUCOSE DEHYDROGENASE [FAD, QUINONE]; 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:UP000053825}.
FT DOMAIN 315..329
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOC66688.1"
SQ SEQUENCE 607 AA; 66900 MW; F25AEA4A51F3DF6F CRC64;
DFSIPLPVCA NPYIGGPQLT DVCSANTGTL FLTLLNTFMI TNIKIGEICG RFTPIDEPEE
SYDFIVVGSG AAGSIVASRL SEIEDWNVLL VEAGGDEPAG SEVPSNLQLF LGGKLDWQYH
TTNESYACLS TNGSCYWPRG KNFGGSTLHH GMAYHRGHAK DFERWVELGN EGWGWDDVMP
YYLKSEDNRE IGRVSPKYHA TGGLMTVERF PYQPPFAWSI LDAADEAGFG TTEDLVGEKI
TGFTVAQTIS KDGVRETPYR SFVERFRDRK NLHVMDNSLV TKINFNMNKV TGVDILRNGT
KYRVNVKREV IVSGGAINSP QLLLLSGIGP KEHLESKNVP VVHDLPGVGE NLHNHQSFGI
DYVLDEDYYS ELNEKSANQY IYNQTGPLSC TGLAQVTGIL ASNLTTADDP DIQIFFAGYQ
AVCNPKENIA DLGVHGSKQS VRFTSVNVRP TSRGRITLNS NNPQDPPIIW SNDMGNEHDR
NVVVQGIHAI LKLAETETMK KLGLTMQHKV IPQCAEKSEP YTDEYWLCAV TYDTRPENHQ
TGSAKMGPKS DPMAVVDLRL RVYGVEGLRV ADASAIPIVV SGNPVASINM VGERVADFIK
EDWGVKN
//
