ID   K1XYL7_MARBU            Unreviewed;      1803 AA.
AC   K1XYL7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:EKD17934.1};
GN   ORFNames=MBM_03706 {ECO:0000313|EMBL:EKD17934.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD17934.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD17934.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD17934.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; JH921434; EKD17934.1; -; Genomic_DNA.
DR   RefSeq; XP_007291595.1; XM_007291533.1.
DR   STRING; 1072389.K1XYL7; -.
DR   GeneID; 18759641; -.
DR   KEGG; mbe:MBM_03706; -.
DR   eggNOG; ENOG502QSPJ; Eukaryota.
DR   HOGENOM; CLU_002483_0_0_1; -.
DR   InParanoid; K1XYL7; -.
DR   OMA; PTGMYHL; -.
DR   OrthoDB; 1945480at2759; -.
DR   Proteomes; UP000006753; 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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT   DOMAIN          590..638
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          664..893
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          1075..1139
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1803 AA;  199645 MW;  AF18A24141B1ABDF CRC64;
     MADLAPTTSS RQEIMSESAN SDSEQHEYLR SSQTFPSNST FEQCQSQIEL NNFGESLGAA
     AKAVFPDEIQ PPYTNVYALM IVWRDEDENR AAPVEVAKLS AVFKDIFKFD VEHFRIPREN
     PQQAVDEKIR GFLDLGGNRA EDLKIIYYAG DTKAKREERV MSTRCAELLT DERMCAYIYS
     GRKKSNPTGD WIDVQTAPEQ AHSDVLILLD SPYTGPSSIS HCSGVTEVIA SRSLNEGAKI
     DKPFAFTEDL AIELRDLSKL PSFSVGNLYH NLFCRSQIRQ SEHPDKPPAP VYAPLNQEND
     RYPRSIRLAI HKDDAHAKGS FEVHHPNPEG VTNLSLSPSF LHSSALIPGS QAPRMAFALH
     ISSRFKVSDL PSSPFQQWLG NLPASLADVK IETGFHSFPS LLVVSAPLFM GIYMPRDPAV
     MHLGPFTGFN EILSGPGAFP PTPTPDIGIF ERPNPSPKIN GIDVPLQQSN GVNGTHISSG
     VRFEELPGAT NGKENKPPFE RGDSQFSLDT SFDTIFDTPI LSSGLRHAPT LHGEIPEKSH
     PIQSPGPHAS EPNGPQSKAH AKIRTYTDDP YTKQFPRISR SVELLRNSYD CIVIGSGYGG
     GVAASRMARA GQSVCLLERG KERWPGEYPS GFLDALKNLH VSGEFAPGFL EGAMVEGGDP
     TGLYHLICGK GQNAFVGNGL GGTSLLNANV FLEADSKTMK MSCWPKELRK PDSLKEYYDR
     AADVLEPETY PDDWPELPKL TMLERQAKAL GWGEKFRRVP QTTRFKGGPN STGVEMYPSA
     LTGMDSTGVN DGSKSSTLVN YLSDAWNWGA EMFCECEVRY IKKHPDPEQE GYLVFFAWHG
     SSRGAFQERL YEDLMWVHAK KCVFLGAGSI GTTEILLRSK KLGLGMSDKV GTGMSGNGDI
     LAFGYNTDSE VNAIGRQYPS PYKPVGPTIS GIIDCRDDHD NPLDGFVIQE GAIPKALAPL
     FQTMLELMPG NQLPTGQTLL EKVKHSIAQQ GSRFLGPYYA KGSIERTQVY LVMSHDSNQA
     ILTLKNDKPV LEFLGVGRSE HVEYLNDVLR QATQAVGGTY VNSPFYAALG QQEITVHPIG
     GACMSKSDSG EHGVTNHWGE VFAGDGKETH HGLIVTDGAV IPTALGVNPF ATITALAERS
     VEHAAKFRIK RRIDFETKNN MLDLFAEPHQ YASAKKVLQR SDTTGIREAT SLVTRTREAK
     SNGFGFSEVM SGYIHVGEGI EGCKIEDYQT AAKTAKGLCE EARFFLSVKA WDTETIVNKA
     DHSAMLTGTF TCAGLPGSPF MVQRGAFHLF SVDSEAPGTR NLTYDFDMTS TDGGAFHFHG
     QKIVDSSVAL GPWRFWKATS TLYVTISEAN GGKRVLGRGM MHIKPMDFLS ELFTLKPSGK
     SFLSKLHSSV SFMGFFAKQS MGLFLAPFTW QQYPSVTYSG FINETSPDRT IKIVASDGVQ
     TFLHIWEPRN PELKTENLFM IPGASVDHQI FSLPTIDVNA VNYFTRAGYR VHVTVHRICQ
     LMIAENDWTT YDSRLDIRAC YEWMRKEHGH APIYTISHCM GAVAFSSGLL DGTIPAKWVR
     GITSSQVLMN PIWSTLNMAK VMAGPVPFDK LYGWLGGKWF SCSSTRGDSY FQQLVNQILR
     FYPDAREEIC NNVSCHRCSL IFGRLWNHRN LNDATHRQLN RFFGGVNMTC LHLLMQMGRR
     GLVTTNSPLF GDLTTPAHLR RLARLPVMLF SGADNQVLTP EATERSYGLL RDAFGPANYS
     RHLIQGYGHL DCWMGREAYV DVFPRVRAEV DRVCRGETYR YAEPDWEAER ARGVSWRDLP
     VSS
//