ID A0A1V6RY77_9EURO Unreviewed; 618 AA.
AC A0A1V6RY77;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=PENVUL_c018G02762 {ECO:0000313|EMBL:OQE06434.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE06434.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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, ECO:0000256|RuleBase:RU003968}.
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:OQE06434.1}.
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DR EMBL; MDYP01000018; OQE06434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RY77; -.
DR STRING; 29845.A0A1V6RY77; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000191518; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT DOMAIN 99..122
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 290..304
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 618 AA; 67853 MW; F9AF41C0967A8001 CRC64;
MTKDDTQGRT CSLEEFFDTA FDYIICGGGT AGCTVAARLS ENAQVTVGLI EAGKCRLGDP
VVDTPARFGE MFDNPEYDWC IYTEPQRENH DNVHHVPCAK FLGGSSGMNA TCYVRGSLQE
YDDWAGLVGD EGWSAEAMQQ YMRKHQTFEA AEADLGRSIN SLSKFHGLQG PIHTSFNDAV
LPIEHAFIKA CEEATGITKR PEDPWSGDHM GFYHGLTTVN RTGPNKGKRS YAAGAYLESN
HTRSNLKILC ETRVNKVILD ENHRATGISI THSENDYEVT VAQEVILCAG TIFSPHILEL
SGIGDPAVLE RAGIPCKVEN FAIGTNFQDH AMSFTTWHVQ PDVITGDILR LVPEAMHSAI
NQYVETKDGP LTNAPIVTGF LSAKSVMAEA ELNGLIQNIM EIKPANAFHA KQLKCIIANL
QDKNSANLQI SIMPLMTNPK RDSRHHKELF VLGPEWQGRG ITLVVGIQYP VARGYIHVEC
DDFACPPMIQ SNLLGHEADV TLLAAALRWA DTVGRSEHLQ DSISSRSFPH PEVDLQNLDR
AKEAVHEFVN SNYHVCGTVA LGEALDTRLR VKGVQGLRVV DASIFPNNVS GNIQATVYAV
AEKAADLIKE DWGLLARE
//
