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Database: UniProt
Entry: A0A1D2MA51_ORCCI
LinkDB: A0A1D2MA51_ORCCI
Original site: A0A1D2MA51_ORCCI 
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}.
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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
//
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