ID A0A1F5LGU4_9EURO Unreviewed; 680 AA.
AC A0A1F5LGU4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=PENARI_c010G11809 {ECO:0000313|EMBL:OGE52433.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE52433.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE52433.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE52433.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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:OGE52433.1}.
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DR EMBL; LXJU01000010; OGE52433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LGU4; -.
DR STRING; 1835702.A0A1F5LGU4; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000177622; 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 Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..680
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009519574"
FT DOMAIN 384..398
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 20..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 680 AA; 74037 MW; 6BE53DF9DD28C27F CRC64;
MRLSAVAGLL STLSVVLASG HSSNPRHHDT YKRSPVGGKT TGDNATSTEY DYVVVGSGPG
GGPLAARLAI AGYRVLLLDA GDDQGNATQQ IVPALQLQST EYDPMRWDYF VNHYSNMSRQ
EEDTKMTYRT PAGELHVGRD APDGSEPLGI LYPRAGTLGG CSAHNAMITI YPYENDWEQL
AALTGNDSWS ASNMRKYFER LERNRYIPSG LVGHGFEGWL TTSLTDLRLV IEDQKLLSLI
LAGATAAGQS LLGKLVNTVT GLAGVLLRDL NNASPTRDYE TGPYQVPLAV DVPEYKRTGP
REFLMKTVNA VNSDGSRKYH LDIQLNTLVT KVRFDTTGAK PRALGVDYLR GQSLYRADPR
ASRTASNGIP GSVNAAREVI LSAGSFNTPQ LLKLSGIGPQ EELSELGIST LVNLPGVGSN
LQDRYEIGTV GKSPTDFVLT SKCTFMYTMP DPCLEQYEND PLFKGTYTTN GIAIAIIRKS
SVAVDEPDLL ISGAPVNFPG YYPNYSYEGL KDAQHWTWIT LKARSRNNAG TVKLRSTDPR
DVPDINFNSF DTGVTENDAD EKDLQAVYEA VEFSRTIFED LIPLDGGFDE VWPGPNVTTE
SEVKNFIKQE AWGHHACCTA AIGEDGDEKA VLDSDFRVRG VNGLRVVDAS VFPKIPGYYV
ALPIYMISEK AAEVIIADAA
//
