ID A0A1F5LA32_9EURO Unreviewed; 593 AA.
AC A0A1F5LA32;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENARI_c018G06442 {ECO:0000313|EMBL:OGE50064.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE50064.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE50064.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE50064.1,
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|ARBA:ARBA00001974};
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:OGE50064.1}.
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DR EMBL; LXJU01000018; OGE50064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LA32; -.
DR STRING; 1835702.A0A1F5LA32; -.
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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622}.
FT DOMAIN 10..312
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 430..567
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 593 AA; 65753 MW; 08AE08A33E881044 CRC64;
MAFVSNGSEY DFIIVGGGTA GNAVAGRLAE NPEVRILVVE AGIPNPDQIQ QITTPSKAFT
LRGSKYDWSY KTTMIKRDDY ERVEKPNTRG KTLGGSSCAN YFTWIPGSKP TFDDWEAFGG
RDWNWDSCVE YLRKCATYHD EEKLYPAELS KIGTGGPVQI SHADLVPEMK PFRDALTEAW
VSKGQPLSED IYSGEMKGLT HCVDTIYRGE RQGSFLYLKN KPNVTILYGV QSKNLIIDPA
TRICSGVTVI SEAAGQEISI YASREVILSQ GVFETPKLLM LSGVGPTAEL AKHGITPIVE
SPHVGQHLLD HPIVPFVLEV KDGYSLDDYV LRPGPLNDKA LSTYQKDKTG PASSGFLELV
GFPRIDERLE KYPAYREAKA ANGGLDPFGP AGQPHFELDF VGLFSTAFQW HYPMPEKGSY
MTCIVDLLRP LSEGEVTLNS SNAQIQPNIN LNFFGNNLDI LAMREGVRWT YDILTKGAGF
KDIVVSEYPW KMPLQSDEDM NRAVLDRSQT GFHPCGTARL SKSIHQGVVD SKLRVHGVRN
LRIADASVIP VIPDCRIQNS VYMIGEKGAD IIKSEHKDLY ESKNIPYHVS SRL
//
