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Database: UniProt
Entry: E2BKW7_HARSA
LinkDB: E2BKW7_HARSA
Original site: E2BKW7_HARSA 
ID   E2BKW7_HARSA            Unreviewed;       533 AA.
AC   E2BKW7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Glucose dehydrogenase [acceptor] {ECO:0000313|EMBL:EFN83663.1};
GN   ORFNames=EAI_01051 {ECO:0000313|EMBL:EFN83663.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN83663.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN83663.1,
RC   ECO:0000313|Proteomes:UP000008237};
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; GL448836; EFN83663.1; -; Genomic_DNA.
DR   RefSeq; XP_011140803.1; XM_011142501.2.
DR   AlphaFoldDB; E2BKW7; -.
DR   STRING; 610380.E2BKW7; -.
DR   InParanoid; E2BKW7; -.
DR   OMA; GINYMMY; -.
DR   Proteomes; UP000008237; 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; 2.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
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:SF154; FI04917P; 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; 2.
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.
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:UP000008237}.
FT   DOMAIN          82..105
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   BINDING         84
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   533 AA;  59499 MW;  C7E6594452B8C686 CRC64;
     MQQYDYIVVG AGSAGAILAA HLAEDEHKVL LLEAGGTAPP FLSIPLLAPA IQKTVYDWQY
     VTVPQKYACR GLINNQSIWP RGKVLGGSSR LNYMAYVLGH KLDYEEWFPD FLQTVAENND
     SVSTSELRWQ SDFANVILEA IKELNYDIGN MNKKLTTGFM KVQLTMENGE RWSSEKILHK
     KCKYSPVILT HTFATKVLVN LNKAEGIEFV RFGSKYTAVA KKGVILSAGV IESPKLLMLS
     GIGPRKHLND LNIHVINDLP VGQNLVDHIL TGVDLVTLNV SLGLNLFQIL NPVSALNYFL
     FGRGQWTSTA IEVLGTFHSV ANKNKSAIPD LQLMVLSLGI SNDNGIIFKK AMGFSDEVYN
     KYFTPLLYEN TIIIAPILLH PKSSGELRLR SNNPFDKPLI DPQYLSNEDD IETLVEGLYF
     VKDLLETNAL RAYSASLNKK SFPGCENETF DTREYWRCYM RHLTLTAYHP AGTCRMGDVV
     DTSFKVHNMT NLYVVDASVL PLLPSGNINA AVIALAQKAS RIFRNEKIKE KEV
//
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