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Database: UniProt
Entry: A0A428QTR1_9HYPO
LinkDB: A0A428QTR1_9HYPO
Original site: A0A428QTR1_9HYPO 
ID   A0A428QTR1_9HYPO        Unreviewed;       595 AA.
AC   A0A428QTR1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CEP53_002463 {ECO:0000313|EMBL:RSL68784.1};
OS   Fusarium sp. AF-6.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL68784.1, ECO:0000313|Proteomes:UP000287544};
RN   [1] {ECO:0000313|EMBL:RSL68784.1, ECO:0000313|Proteomes:UP000287544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL68784.1,
RC   ECO:0000313|Proteomes:UP000287544};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:RSL68784.1}.
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DR   EMBL; NKCJ01000033; RSL68784.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428QTR1; -.
DR   STRING; 1325737.A0A428QTR1; -.
DR   Proteomes; UP000287544; 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:UP000287544}.
FT   DOMAIN          10..312
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          430..568
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   595 AA;  65856 MW;  7D413AA7D5C28AA7 CRC64;
     MAFVANGNEY DFIIVGGGTA GNAVAGRLAE NPNVRILVVE AGIPNPHQVP EITTPSQAFN
     LRGSKHDWAY KSTMIKRDDY ERIEKPNTRG KALGGSSCAN YFTWIPGSKP TFDDWEEFGG
     PEWNWDNCVD YLRKCATYHD DEKLYPAELK KIGTGGPIQI AHADLVPEMQ SWRDALTQAW
     VSKGEVLTEN IYDGEMRGLT HCVDTIHGGQ RQGSFLYLKN KPNVSILYGV QSKQLIIDPH
     TNACLGVTVI NPANNNELSV YASREVILSQ GVFETPKLLM LSGVGPAKEL SKNGVDVKVD
     SPHVGQHLLD HPIVPFVLKV KDGFGLEDYI LREGTTNSAA VAQYKRDKTG PIGSGLLELV
     GFPRIDERLE KHQAYREAKA ANGGLDPFGP AGQPHFELDF VGMFSTAFQW HYPVPEKGNY
     MTVIVDLLRP LSEGEITLNN ADPLVQPNIN LNFFANDLDI LAMREGVRWT YDVLTNGAGF
     KDIVVGEYPW RMPLESDAEM KRAVLDRSQT GFHPCGTCRL SKSIQQGVVD SRLRVHGVKN
     LRVVDASVIP VIPDCRIQNS VYMIGEKAAD MIKSDHADIF AEGAFKNIRS FTSRL
//
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