ID E1ZVM3_CAMFO Unreviewed; 623 AA.
AC E1ZVM3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Glucose dehydrogenase [acceptor] {ECO:0000313|EMBL:EFN74792.1};
GN ORFNames=EAG_10201 {ECO:0000313|EMBL:EFN74792.1};
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:EFN74792.1, 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}.
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DR EMBL; GL434548; EFN74792.1; -; Genomic_DNA.
DR RefSeq; XP_011251213.1; XM_011252911.2.
DR AlphaFoldDB; E1ZVM3; -.
DR STRING; 104421.E1ZVM3; -.
DR EnsemblMetazoa; XM_011252911.3; XP_011251213.1; LOC105248237.
DR EnsemblMetazoa; XM_025407863.1; XP_025263648.1; LOC105248237.
DR EnsemblMetazoa; XM_025407864.1; XP_025263649.1; LOC105248237.
DR GeneID; 105248237; -.
DR KEGG; cfo:105248237; -.
DR InParanoid; E1ZVM3; -.
DR OMA; ECARGKV; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000000311; 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: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; 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:UP000000311}.
FT DOMAIN 310..324
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 273
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 623 AA; 69493 MW; F00ECDA7B8E1C0F3 CRC64;
MGVESILAGS LASATNGLSW FFPILAAVLV YFQYEALNDE APLIDMPSEV LLPTYHFIVV
GGGSAGAVVA NRLSEIEDWN VLLLEAGGDE TEISDVPLLA AYLQLSQLDW QYKTEPQGDA
CLAMENNRCN WPRGKVMGGS SVLNYMLYIR GNMRDYDIWE QQGCTGWGSP GVLYYFKKSE
DNKNPYLIRT PYHASDGYLT VQEAPWHTPL ATAFVQAGQE MGYENRDING KYQTGFMIAQ
GTIRRGSRCS SAKAFLRPVR MRKNLHVAMH AQVTKVLVHP ESKRTYGVEF MRNGKMFRIR
ASKEVILSAG AINSPQILML SGIGPKEHLQ ELGIPVLQDS RVGYNLQDHV GVGGLAFLIN
QKISIVQNRL QNIQTAMQYA ILGDGPLTIL GGVEGVAFVN TKYMNASLDF PDIELHFVSG
STNSDSGVQI RKVHGLTKKF YDAVFGPIND KDTWSVIPML LRPKSRGMIK LRSTNPFDHP
LIYPNYFKEP EDMATLIEGV KISVALSRTN AFKRFGSELN PRQFPGCEHI PMFTDQYWEC
MIRYYSVTIY HPVGTCKMGP YTDPEAVVDP QLRVYGVAGL RVIDASIMPN LVSGNTNAPV
IMIGEKGADM IKEYWLKQKM FNK
//