ID Q2H2M4_CHAGB Unreviewed; 621 AA.
AC Q2H2M4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=CHGG_03972 {ECO:0000313|EMBL:EAQ87353.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ87353.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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}.
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DR EMBL; CH408032; EAQ87353.1; -; Genomic_DNA.
DR RefSeq; XP_001223186.1; XM_001223185.1.
DR AlphaFoldDB; Q2H2M4; -.
DR GeneID; 4392061; -.
DR VEuPathDB; FungiDB:CHGG_03972; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_0_1; -.
DR InParanoid; Q2H2M4; -.
DR OMA; DPRYCAD; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000001056; 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:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 2.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..621
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004208438"
FT DOMAIN 250..264
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 340..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 544
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 587
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 109..112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 209
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 621 AA; 65267 MW; 3A7756BE27557D1A CRC64;
MVLVPLMMFF LFQVFLSPAD SLLIRPHETD ELTLSSYDYI IVGGGVSGLV VANRLSEDSN
DIVTVPGLIG HGFPPAYNWN FTTAPQEFLD SNTRDYGQGH VVGGGSILNG IVTTRGARAD
YDAWEALGNP GWGWQDMLPY FKKSVHGTSG PLEVTYPNFL YNQSRVAVGA MIAPASMSAS
NQSRMDSRTA YLDPVLYRPN LHLAVGQTVT RLLIESNGTA NTAAPPFYTT SAESLHRQVW
CGREVILAAG AIISPALLQV SGIGPADLLN ELGVPVKVDL PGVGQNFQDH PMVGVFYNCP
WTSPLITTIA FAHLSHLTAN NNTTTTTTNT TASLLTALLN TTTPNPNTNT NTSSPSPNPN
PNPNPNPNSL QYLPHTTTRH KTLLAGYTAQ LTLLGSTLLP NPAVAALELL ADSLGTLTVA
VQHPLSRGTV RALSADLLLL GGDGGHNGGG EGGGGGGGVA RNIALDPRYC SHPADCALLV
AGVGMSGRVA GTRAMRELRP RPEVGLAVSS FGSGGGDGGG DGANGDDGKE VLEMVKRRVQ
TEFHASGTTA MMPLHLGGVV SKRLVVYGTA NVRVVDAGIM PLVVGAHIQA AVYAVAEKAA
DLIKEDNKRN VGRHLKSRKG N
//
