ID   V5EWS1_KALBG            Unreviewed;       596 AA.
AC   V5EWS1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=PSEUBRA_SCAF1g00495 {ECO:0000313|EMBL:EST10040.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST10040.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; KI545851; EST10040.1; -; Genomic_DNA.
DR   RefSeq; XP_016295029.1; XM_016436057.1.
DR   AlphaFoldDB; V5EWS1; -.
DR   STRING; 1365824.V5EWS1; -.
DR   GeneID; 27418686; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_7_1_1; -.
DR   OMA; NHFESCA; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000019377; 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   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377}.
FT   DOMAIN          311..325
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         135
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   596 AA;  65306 MW;  1E20AB6BDDF63B77 CRC64;
     MAPKPNPARP DTDPVHGQTV ENHPANPNPS SSSSGPTARE RLASLASHLL PGGNTEFDYV
     IVGGGTAGAV LANRLTEDRN VSVAVIEGGP TDVGNDMVLD LSRWLEMLGS DLDYDYPTVP
     QPRGNSFIRH SRARVLGGCS SHNTLISFRP FNEDLDDWAN NYACPSWSAS TVQPYGDRLK
     MNIVPVAPQQ RNQVARDWVT ASSRATGAPV LEDLNAHIVH RGGFQKAVGF FDIAYDPYSG
     QRSSASVAYL HPIMPHGPYK RHNLHLFLET WANTLEYAAN DAAKVTGVKV TTKHGLSKTL
     TARREVILCA GAIDTPRLLL HSGIGPRGDL EKLGLPCKHD LPGVGLNLTD HPESIVMWET
     RDTPPETVMS SDAGLFLRVL PSDAEPNPHP GPDLMFHIYQ VPFADNTERV GYERPKHAIC
     MTPNICRSQA RGKVSLASAN PKDKPLLDFK YFEDKDNYDE RILIEGVKWA RKIAEMSPFK
     EHLVKEVAPG PKIQSDRDIG EYARKVAHTV YHPAGTCRMG TVSRGKGGQG TDESVVVDER
     DLSIVGLKGV RVCDASVLPT LPTINPMLTI LMVAERAAEL IRDDAWFNGL RKTNYH
//