ID F4WRC8_ACREC Unreviewed; 648 AA.
AC F4WRC8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:EGI63345.1};
GN ORFNames=G5I_08374 {ECO:0000313|EMBL:EGI63345.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI63345.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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; GL888284; EGI63345.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WRC8; -.
DR STRING; 103372.F4WRC8; -.
DR EnsemblMetazoa; XM_011059868.1; XP_011058170.1; LOC105148247.
DR eggNOG; KOG1238; Eukaryota.
DR InParanoid; F4WRC8; -.
DR Proteomes; UP000007755; 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:UP000007755};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..648
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003318883"
FT DOMAIN 355..369
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 648 AA; 72757 MW; 3048906079E214E8 CRC64;
MFRYDMRWYF LCLILAHYVI ATPVKEHQPI QASNDYGTNG CCLCQFEDTQ YMSNVCGDGS
SFMTLIQHIL SSKCDIADPC RRLGRDEAPI EYEWFDYIIV GAGVAGPIIA RRLSETSWQR
VLLIEAGPEE PSMTAIPAFM LNTINTSLDW NFKTESTESH PTACLETGGV CTWPRGKMVA
GTGAMHGMMY YRGHPEIYNH WAREGNLDWS YDEISHYFER VENPVHPTIL SDKPRSLKEG
GPMNIQYYPH KPDFANVLLT AASELGYRTS LLKEYNQTGF MIAPMTIENG MRLTTSKAYL
RPVHDRKNLR VLTNAQVTKI LIRPWEQKAY GVELVDKNGY KRVVKCDKEV ILTAGAIGSP
HILLNSGIGP EKDLAKFGIK VFKDLPVGKN LHNHVSVGVP MSIKDIPYEI MTMDAVNKFL
ENKTGPLTST GLTQITGFLE SSYAINGVPD IQVFFDGFIP ICSKTGLVNE CINDKFQSDC
PDRRKIVVRP TVIFAESRGD LKLRSNNPLD PPLIYPNYFT KEKDLMILLE GIKKVSKFVD
TPTMKKWDLR LEQVRSPLCS DYHFGTDAFW LCQIRAKTGP ENHQSGTCKL GPSTDPSAVV
DSQLRVHGIS NIRVADASIF PIVPNSNPIA GIMMVAEKAA DMIKNTWL
//
