ID   A0A0N0U691_9HYME        Unreviewed;      1631 AA.
AC   A0A0N0U691;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   SubName: Full=Glucose dehydrogenase [acceptor] {ECO:0000313|EMBL:KOX76352.1};
GN   ORFNames=WN51_11683 {ECO:0000313|EMBL:KOX76352.1};
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:KOX76352.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX76352.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX76352.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX76352.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ435750; KOX76352.1; -; Genomic_DNA.
DR   STRING; 166423.A0A0N0U691; -.
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: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   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|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1631
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005859867"
FT   DOMAIN          1137..1160
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          1312..1326
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   1631 AA;  183931 MW;  DC454B1716D1E7C5 CRC64;
     MKGFYNCSNI FILCLILGTI DGNDHRGCAY LQCRGSDVCV HRKFRCKDPP CPSMLYCARS
     RTESLRGPST CDTVHCTNGY MCTLKVRRCH WDEKCEQQIA RCVSQKEYYE GPASCAGFKC
     PQGNHCILRE SFCVNPPCKL IQTCMKNKDV QLLFVKCRNL GCPSEYECFL RKPESDCASP
     PCRHTPDCIM ATESCETNDC NIKRICHESH AVAANDSSSS FSRRSLKNKD EGSLNDTEQF
     EDWLRSIKDI LGPAAYSGWL EEILSSRGEQ LRKWLRTSHD KLNAGGPIFP GQERPGGTLT
     ENPYVVGDTM NTSPSDDSNK EIETFVSLLR ERNLTNILER ILVPSRVLLP PYVTLETALL
     NNPRESDPSS FSAHLLKYPS HVGSQFLSLR PRKTESTYDQ RYLVVPVKNM KELTNSQIID
     YDSNIRHYHE ITPESGKMSD ERDNSYSINC FFKNVPERKI NLSSTRDDNS SLKTGLYEDF
     EKKLPKKETH SEDSIGLLGD KRLMGKAQHF DDVPVDFLEK FLKSMQLFPI ENVPQTFDEK
     SIEEYRQDDS SKAPQNEKHD ENFEWDLTFR NKNSEESEHQ FFFSNDDYKN FTSNVEPSVN
     TFFDKLAQID NNENEKIDLN LFFELNKESL LPYIQTILEM MNEEHDTSSR EAELNFDESS
     LKTSVLNNEE VAPGVINCNE SESLKTESNN VKKVLNNDSQ VLEGETFDKT FLKTQIETAS
     TNSKLQQERE SGTPELIYAN EEPTIRSFYN LPSYGASNDE TAFQDYNIHF EYNRMKRKNG
     HEKSSERGKI APHERFYDAR TYLVRNNERR ASGQPLPSGR PENNIHYSPN TLHYNKCQRA
     VNLKARAEMN HERKIVAKAD LMFFNFQRRN GSDRTDHFHK LVPWQKGSVD INESRAGDAD
     TILFPGDQES MNGLSAGKTT LIRLLKFLAT IITVHNVERR ASLNVESENE SRRKRKRKTW
     KNVAAPLQGQ TTMSCNCPLT PSTGPTLAST CGGSSFMLFM GLLEVFLRSQ CDLEDPCNRP
     LSASSVNSRH ASRITVQKLE TSLSSLSLSE ASVHNIQYDF VVIGGGSAGA AVAARLSEEP
     RFSVLLLEAG LDEPTGTQIP SFFFNFIGTN IDWQYNTESE DTACLNKDDR RCYWPRGKVL
     GGTSVMNGMM YMRGSRKDYD DWARLGNIGW SYQDVLPYFI RSEDNLQANI MDYGYHGVGG
     PLTVTQFPYH PPLSYSILEA GKELGYGTAD LNGRTHTGFA IAQTTSRNGS RLSTARAFLR
     PARNRSNLHI MLNSTATRIL FDNNKRAVGV EFVHDGEIHR VSLAKEVVVS GGAVNSPQIL
     LNSGIGPRED LNAVGVPVVH DLPGVGKNLH NHVAYTLTFT INDTDTTPLN WATAMEYLLF
     RDGLMSGTEQ KNVAKAHQIM GVASETIERV CIQWAVKARI SEVTAMINTK YANPKVDHPD
     VQLIFGGYLA DCAETGMVGE TKGANRTIYI IPTYLHPKSR GYLRLRNNDP LSKPLIYPKY
     LSHPDDIAGM VEAIKFGIKL AETEALSRYG FQMDRTPVKN CEHLKFGCDE YWECAVKHET
     SPENHQAGSC KMGPPDDPLA VVDNQLRVRG VRGVRVADTS IMPRVISGNT NAPAIMIGER
     AADFIKRTWI G
//