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Database: UniProt
Entry: E2ASE9_CAMFO
LinkDB: E2ASE9_CAMFO
Original site: E2ASE9_CAMFO 
ID   E2ASE9_CAMFO            Unreviewed;       630 AA.
AC   E2ASE9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Glucose dehydrogenase [acceptor] {ECO:0000313|EMBL:EFN63615.1};
GN   ORFNames=EAG_07393 {ECO:0000313|EMBL:EFN63615.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN63615.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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; GL442298; EFN63615.1; -; Genomic_DNA.
DR   RefSeq; XP_011263210.1; XM_011264908.2.
DR   AlphaFoldDB; E2ASE9; -.
DR   STRING; 104421.E2ASE9; -.
DR   InParanoid; E2ASE9; -.
DR   OMA; NYPWIHI; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
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   630 AA;  70118 MW;  6B5E1AFE1190A7FD CRC64;
     MVFSTIIVTS ALKGAISLMG TGLWLVPLLI AGLSYYHYDQ LDPESRPIDR YPLYSNYDFI
     VVGGGSAGAV VASRLSEIPD WNVLLLEAGP DENEITDVPS LAAYLQLTKL DWKYKTEPTG
     KACLAMKGGR CNWPRGKVLG GSSVLNYMLY VRGNRYDYDH WESLGNSGWG YKQVLYYFKK
     SEDNRNPYLQ KSPYHATNGY LTVQESPWKT PLVVAFIQAG VEMGYENRDI NGERQTGFMI
     SQGTIRRGNR CSTAKAFLRP VRLRRNIHTA INSHVTKIII DPLTMKAIGV EFVRDGRKQM
     VRARKEVILS AGAINSPQIL MLSGIGPKEH LRHIGIPVIE DLRVGDNLQD DVGMGGLAFL
     IDKPVVIVQD RFQSAPMTMH YVVNGRGPMT ALGGVEGYAF VNTKYANYSI DYPDLQFHMA
     PASINSDAGV QVRKIFGLTD EVYNTVYRPI TNKDAWTLIP VLLRPKSRGT IRLKNSNPFH
     SPLINANYFS DPMDIAVLVE GVKIAIKISE AKVFKQFGSR IHRIKLPGCK HFKFGSDAYW
     ECHIRHISET IYHPVGTAKM GPPTDPTAVV DPRLRVYGIT GLRVIDASIM PTISSGNTNA
     PVIMIGEKGA DLIKQDWLRS SSGNNHESVY
//
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