ID A0A094EC32_9PEZI Unreviewed; 692 AA.
AC A0A094EC32;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=V499_05941 {ECO:0000313|EMBL:KFY73993.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY73993.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY73993.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY73993.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
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:KFY73993.1}.
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DR EMBL; JPKB01000987; KFY73993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EC32; -.
DR HOGENOM; CLU_002865_4_1_1; -.
DR Proteomes; UP000029295; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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:SF213; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
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|PIRSR:PIRSR000137-2};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..692
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001901147"
FT DOMAIN 393..407
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 692 AA; 74267 MW; 89C89016D8728F67 CRC64;
MLSLLPLSVF LSFTSTVLAA YVIPQNVTLK KEAGTNCPSA LHNHPHEGHS KRQADSNTTW
LENYEYVVVG SGPGGGPVAA NLAIAGFKVL LIDAGDDQGG ALQYQVPALQ LQATEYEPMR
WDYFVNHYSD EARQQKDSKM VYQTTSGEQY VGLNPPSGST PLGILYPRAG TLGGCSAHNA
LITIYPHDSD WTNIATITGD NSWSPDKMRK YFMKLERNRY LPSSIIGHGF DGWLGTALTD
LSLVIEDPKL LSLIIAAGTA MGKGLLGLLV NTVGGLGQVL LRDINAPGQS SKAGLYQVPL
AMADSKRNGP RNLVLDTANA VNKDGSRKYH LDIKLTTLVT KVRFSHDGPT PKAVGVDFLD
GQSLYRADPR SGSATVTGSG SVNATREVIL AAGAFNTPQL LKLSGIGPAA ELESFDIPVV
VDLPGVGTNL QDRYENTIIG DSPTDFFITK KCTFMETMPD PCLTRWTNGI GPIAKGTYGT
NGIAIAIVQK SSVAEGEPDL LISGAPAKFK GYFPGYSSDS LHDAHHWAWI VLKAHSRNNA
GAVTLRSTDP RDMPNINFNY FDTGVTANGA ADKDLQAVYE AMKFSRKIFK GLIPLDGGFN
EVWPGPNVTT EADMKEFIKD EAWGHHASCT CPIGADGDPM AVLDSNFKVR GVEGLRVVDA
SVFPKIPGFY ISLPIYIVSE KASDVIIQAA AA
//