ID A0A0M9AA24_9HYME Unreviewed; 624 AA.
AC A0A0M9AA24;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE SubName: Full=Glucose dehydrogenase [acceptor] {ECO:0000313|EMBL:KOX80305.1};
GN ORFNames=WN51_07970 {ECO:0000313|EMBL:KOX80305.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX80305.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX80305.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX80305.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX80305.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KQ435704; KOX80305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9AA24; -.
DR STRING; 166423.A0A0M9AA24; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000053105; 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:SF215; FI02019P; 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT DOMAIN 136..159
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 312..326
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 138
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 624 AA; 69222 MW; D3D75337CE5112C4 CRC64;
MVFSTIVVTS ALKGALSLVG TSLWLIPLLI AGLSYYRYDQ LDPESRPIDR YPLYPEYDFV
VVGAGSAGAV VASRLSEVPK WNVLLLEAGP DENEVTDVPS LAAYLQLTKL DWKYKTEPTG
RACLAMNGGR CNWPRGKVLG GSSVLNYMLY VRGNKHDYDH WESMGNPGWG YDQALYYFKK
SEDNRNPYLQ RSKYHSTGGY LTVQESPWKT PLVVAFVQAG TEMGYENRDI NGEQQTGFMI
AQGTIRRGSR CSTAKAFLRP VRLRRNIHTA MNSHVTRVLI DPLTMRATGV EFVRDGRRQI
VRARKEVILS AGAINSPQIL MLSGIGPKEH LRHIGIPVIK DLRVGDNLQD HVGMGGLTFL
IDKPVAIVQD RFQAAPVTMH YVANGRGPMT TLGGVEGYAF VNTKYANLSI DYPDIQLHMA
PASINSDGGV QVKKVLGITD QVYDTVYRPI ANKDAWTIMP LLLRPRSRGT IRLRSSNPFH
SPLINANYFA DPMDIATLVE GAKIAMRVSE ARVFKQFGTR VHRIKLPGCR HLKFASDAYW
ECHIRHISMT IYHPVGTTKM GPASDPTAVV DPRLRVHGIA GLRVIDASIM PTICSGNTNA
PVIMIGEKGA DLVKSDWLAI ETKR
//
