ID   F8MVE9_NEUT8            Unreviewed;       827 AA.
AC   F8MVE9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN   ORFNames=NEUTE1DRAFT_50117 {ECO:0000313|EMBL:EGO54752.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO54752.1};
RN   [1] {ECO:0000313|EMBL:EGO54752.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO54752.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; GL891307; EGO54752.1; -; Genomic_DNA.
DR   RefSeq; XP_009853901.1; XM_009855599.1.
DR   AlphaFoldDB; F8MVE9; -.
DR   GeneID; 20828249; -.
DR   KEGG; nte:NEUTE1DRAFT50117; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_50117; -.
DR   HOGENOM; CLU_011025_0_0_1; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000008065; 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   CDD; cd09630; CDH_like_cytochrome; 1.
DR   Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF49344; CBD9-like; 1.
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|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..827
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003380654"
FT   DOMAIN          354..377
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   REGION          236..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   827 AA;  88418 MW;  0D2A530F90894FEB CRC64;
     MKVFARIGTI ALAALYLQQC SAQYINEQYT DPVNKITLST WRPDPGSNSG GGDAATYAFG
     LVLPPDALTK DANEYIGLLR CDVGDAASPG WCGVSHGQSG QMTQSLLLMA WASKGQVFTS
     FRYASGYNVP GLYTGNATLT QISATVNSTQ FELIYRCQDC FAWNQGGSKG SVSTSSGLLV
     LGRAAAKGNL QNPTCPDKAI PGFHDNGFGQ YGAPLEKVPH TSYSAWASLA TKTTTADCSG
     ASDPAPTGSE PPAEPTSTAE PVPVCTPAPS KTYDYIIVGA GAGGIPIADK LSEAGKSVLL
     IEKGPPSTGR WNGTMKPEWL QATNLTRFDV PGLCNQIWVD SAGIACTDTD QMAGCVLGGG
     TAVNAGLWWK PHPQDWDYNF PEGWKSRDTV PATNRVFGRI PGTWHPSQNG KLYRQEGFNV
     LANGLSKSGW KEVIPNDAYN QKNHTFGHST FMFAKGERGG PLATYLVTAA ARKQFTLWTN
     VAVRRAVRNG SRVTGVELEC LTDGGLSGTV NVTPNTGRVI FAAGTFGSAK LLLRSGIGPT
     DQLEIVKGST DGPTFISKDQ WIDLPVGYNL MDHLNTDLII THPDVVFYDF YGAWNTPIEG
     DKSAYLQNRS GILAQAAPNI GPLMWDELKG SDNIVRTLQW TARVEGSDQY TTSKHAMTLS
     QYLGRGVVSR GRMAISSGLD TNVAEHPYLH NDVDKQTVIQ GIKNLQAALN VIPNISWVLP
     PPDTTVESFI NNIIVSPSNR RSNHWMGTAK LGKDDGRAGG SAVVDLNTKV YGTDNLFVVD
     ASIFPGMTTG NPSAMIVIAS EHAAQKILAL KPVPSLPGGN GKGKWRR
//