ID A0A1D2MA51_ORCCI Unreviewed; 1134 AA.
AC A0A1D2MA51;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Glucose dehydrogenase [FAD, quinone] {ECO:0000313|EMBL:ODM89866.1};
GN ORFNames=Ocin01_16816 {ECO:0000313|EMBL:ODM89866.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODM89866.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODM89866.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODM89866.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODM89866.1}.
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; LJIJ01002314; ODM89866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2MA51; -.
DR STRING; 48709.A0A1D2MA51; -.
DR OrthoDB; 3386537at2759; -.
DR Proteomes; UP000094527; 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; 4.
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; 3.
DR Pfam; PF00732; GMC_oxred_N; 3.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..224
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 244..308
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 410..481
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT DOMAIN 518..553
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT DOMAIN 652..786
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 990..1125
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 1134 AA; 125638 MW; 28560F8203DB1034 CRC64;
MQNKIVHKMG VVDAVKVILR ALPGRWPLPI PVSVFSATFL TLAINSWVAY DMSRDVKTNN
ELRTKDTKCQ FTTFDYIIVG VIYNSGGAGM VVATRIANAS SSNRILLLEA GGEPSVLNDI
PKSYDHKGKM LGGSTATNFM MYVRGNKEDF NRWSTEDLGG DPQWNYENLL PYFKKSEDYN
GAWANEPDAF KYHGKGGLRN VAKCDYHPGA EELFAAALEK GYSQGITMGQ IRVKFQTCLE
SQKLGVVYKR QGLTRIATAR KEVILSAGTF ESAKILMLSG VGPAEHLRSL NISVVKDLPV
GQNLQDHLIT LVGPFLKAPA VNPNRDVTAQ AAYHYLSTGN GILAASDALA GQDRIMQISS
DTRCLCPLPH LPEDMNKMFG VRVDILKKWF DPYHKNDTDA RFRLLVLGRP KSFGNLTLAS
RNPDDNPIMD PQFLTHPDDV EAMLYGFKKF VDLYENTTAL NTPLFHKPVP GCEAKEFRMC
HSHVLVHTLS SCWDLRFGKG GGWQLEMIEF IFSLLFGHVR VIGIDGLRVI DASVIPREPN
ANTQAATIMI AEKGSDLIIA DITSQCVHEL QLLATLHLVK TFETCRMGVV DAVNTILRAL
PARWPIPIPI SIFTATFISL AINSWVSYDI SQDATVNSEI LTLDSKCQFT TFDYIIVGGG
GAGMVVATRI ANASSSNRIL LLEAGGEPSV LNDIPGLDGF LSNQPANTWF YNSTVQANAC
QNCDGKVNND NARKNVGCST STNFMMYVRG NKEDFNRWST EDLGGDPQWN YENLLPILKN
LRIIMEFMQA TLPQRNTMEK EVFAMWQPMI FSQVLMNFWL LLWKRGIQSG LQWGKSRRDT
GKPSNLCIKN MLMSPKSLSN CFRSAKSYFS NVQTPRSHSN SDCNQRNHPQ RWGYILTFGS
AKLLMLSGVG PAEHLGSLNA AVSYLSTGNG VLAASEALAV IQASFGLYPQ LPQDLNRMVG
IRADILDNWF DPYHKTNTDA RFCLLIAGRP KSFGNMTLAS TNPDDNPIQD PQYLANPDDV
EAMLFGFKKI VDLYENTAAL NTSLFLKPVP GCESLVFKSD DYYRCVIRMF SFTIYHHVGS
CSLGKVVDSQ LKVKGIDGLR VIDASVMPRL PNGNTQAATI MIAEKGSDLI IADM
//