ID A0A139WFX6_TRICA Unreviewed; 1229 AA.
AC A0A139WFX6;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN Name=AUGUSTUS-3.0.2_33430 {ECO:0000313|EMBL:KYB26873.1};
GN ORFNames=TcasGA2_TC033430 {ECO:0000313|EMBL:KYB26873.1};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000313|EMBL:KYB26873.1, ECO:0000313|Proteomes:UP000007266};
RN [1] {ECO:0000313|EMBL:KYB26873.1, ECO:0000313|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB26873.1,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000313|EMBL:KYB26873.1, ECO:0000313|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000313|EMBL:KYB26873.1,
RC ECO:0000313|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; KQ971348; KYB26873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139WFX6; -.
DR STRING; 7070.A0A139WFX6; -.
DR EnsemblMetazoa; TC033430_001; TC033430_001; TC033430.
DR eggNOG; KOG1238; Eukaryota.
DR InParanoid; A0A139WFX6; -.
DR OMA; MPFNTID; -.
DR Proteomes; UP000007266; Linkage group 6.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
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:SF208; GLUCOSE DEHYDROGENASE [FAD, QUINONE]-LIKE PROTEIN; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 2.
DR Pfam; PF00732; GMC_oxred_N; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00623; GMC_OXRED_1; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1229
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007299867"
FT DOMAIN 137..160
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 742..765
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
SQ SEQUENCE 1229 AA; 137679 MW; 456A055B8570E45B CRC64;
MFHSLIWASF LAIFFVLRPV SSNYDDININ TITERFGTIF GTTDPINIIP NHKIDEVYDF
IIIGSGSSGS VVASRLSEIP TWKILLLEAG NAANILTKVP IMAPLFQLTP YNWNYTMEPE
PNVCQAMEEE TCAWPRGKAL GGTSVINYMI YTRGNPLDYQ KWGEVSPGWA FQDVLPYFLK
SENCNLGTAC GSEYHNKGGP LSVEYPFKSP ITDAFLQAGR EMGEEIVDYN TEKYMGFGQL
QANQKFGRRH STFDAFIAPI ITRKNLHIVS GARVTKILID PNTRQTLGVI FEKKGQKYKI
RASKEVILSA GVFNSPQLLM LSGVGPEGHL HDLGIPPIVN LPVGQNLYDH LAFLGVAYTI
NVTVEPREAL LSPLEGLNWF FRGKGLYTSL GGVEAIAYIN TGSLPQANYP DIELIFVGTG
TLQSDFGLVV AKEIRLKRSI YDTVYKPIEN TPSWAIFPML LHPQSKGHLQ LKSTNPHDPP
ILHGNCFTDP GDQDIKTLLA SIRYIQKLAQ TPSFQKFGSK LHDIPLPTCQ KHVFDSDDYW
LCAIKSLSTT LHHQVGTCRM GHWDDPQSVV DPRLRVRGVK GLRVIDSSVI PVTLKMKLQT
VFLLTLLFLV KSDDSENLQY IYDELSAVYG QYSNKTFFLT PDQWAEWTLP KDPGKRESPK
SGYDFIVVGS GSSGAVIANR LSENPNWEVL LLEAGKGENF FSQIPLVCPT LAFTHYNWDF
IAEYQPNVSF GFENNRMRWP RGRALGGTSV INFMIYTRGN RHDYDRWAGQ GNPGWSYRDV
LPYFIKSERS TLNNPHPGVH GTNGYLGVSD IYQSEILRAF IEGGNELGLP YFDYNANEKS
FGVSPIQATV KRGRRHTTAR AFLHPIRHRK NLHMLTSAFV TKVLIDPNTR QTYGVEFSRF
GRKYQVTASK EVILSAGTFN SPKLLMLAGI GPRDHLAEMG IPLLEDLPVG QNLHDHLTYP
GLSFIIDKPL SLSVLHLINP KNIIDFLFNG TGPYTSLGGV GGIGYIKTKE SLEVEDIPDI
ELLFLDGSLS TDYGLWNRRW MNIRDDVYYP VYGPTHNIPT WTIFPMLLHP KSTGYLKLKS
RNPRDYPLLY GNYFTDPAQQ DLKTMLAAIR YIQKLANTRP FQEMGTRMNP NPIPVCAHLI
FDSDAYWMCA IRAISVTLHH QVGTAKMGPK DDPTAVVNHE LKVYGVKGLR VADCSVIPFA
LGAHTNAPAI MVGEKAADLI KADWEKVAR
//
