ID A0A135LQ47_PENPA Unreviewed; 604 AA.
AC A0A135LQ47;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KXG51080.1};
GN ORFNames=PGRI_066520 {ECO:0000313|EMBL:KXG51080.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG51080.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG51080.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG51080.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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}.
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:KXG51080.1}.
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DR EMBL; LHQR01000044; KXG51080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LQ47; -.
DR STRING; 5078.A0A135LQ47; -.
DR OMA; KQTGFML; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000070168; 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; 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:UP000070168}.
FT DOMAIN 276..290
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 84
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 604 AA; 65492 MW; 0C6154C492C4456B CRC64;
MDDYDYIIIG AGISGLVLAN RLSRDASINV LLIEAGANRM GDPRIDTPGF LATMYGNPDF
DWDYMSVPQI HAKNRQIGQP RGRVVGGSSA LNFSAVVYPT VSDFDGWKAL GNDGWGAKDM
ARYLRKFHTY SAPSEATAEL LGTSRYMKVD NQGSSGPLPV SLPDVYGPFN KAWNKTFANL
GWESDADPLD GRKLGAFTCP LSVDAKTGTR GYAAAYYSPD VAARSNLRLL TETVVERILF
KQEDGDVIAT GVQVKSQGNA DSYQITAKKE VVLCAGSLNS PQLLELSGIG GADLLQAHGI
PVIVDNPAVG ENLQDHAITS INFEVADGQV SGDILRDPNV VQALIKLYEE TRGGPLAGMP
LSMAYLPLMD GTGAVPKEEI DTLISKYLDD DNTPANLKAQ YSLLHKMLLQ SDDPSSHYLF
LPAQLHMNPG KTTLTDVLAK TLPENYISIM VLHNHPFSRG SVHISSGKIE DKPTYDPNLL
SHPLDLEIMA RQLQFVGRIA ETAPFSALLK SGKRMPENTT DLSDLDHVKD VVKDRLYTCF
HPAGSCAMLP RENGGVVDSE LKVYGTKNLR VVDASIFPLE PSGNIQATVY AVAERASTLM
KESV
//
