ID A0A3E2GST0_SCYLI Unreviewed; 614 AA.
AC A0A3E2GST0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, 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:PS00624};
DE Flags: Fragment;
GN ORFNames=B7463_g12097 {ECO:0000313|EMBL:RFU24241.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU24241.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU24241.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU24241.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RFU24241.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NCSJ02000481; RFU24241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2GST0; -.
DR STRING; 5539.A0A3E2GST0; -.
DR Proteomes; UP000258309; 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:UP000258309}.
FT DOMAIN 281..295
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU24241.1"
FT NON_TER 614
FT /evidence="ECO:0000313|EMBL:RFU24241.1"
SQ SEQUENCE 614 AA; 67238 MW; C2294D0545876640 CRC64;
MIHTDLDNGF DYIVVGGGTA GLVVASRLSE DAGVSVLVVE AGGDHQGDPA VQIPGLSAKT
LGKEQYDWNF TTVPQAALNN RRIRQPRGKG LGGSSAINFL MTVFPSRGII DAWGKLGNEG
WSYDELAPYF LKFGTRHSPS EEVCQITRTD VIDNHLSGHG PIHMSYGNGF GPMNSAWMDV
HTQLGLKPTG GDLASGQVSG AFQNTFNIDP ATKTRSYAAT AYYGSEARQR SNLTVLTNTI
VQKIELQDQD SEVVATGVQV RMKDGSVRYI QARTEVILGA GALQSPQLLE LSGIGGRALL
EQHGINVVVE NPNVGENLQD HVQVCHSWQC KESIPSRDMF RDPNILQAGI SQYEDNNGDG
PLGRLSISSS YLPMVDIQGR ISEQDKKALL DKYARDATGG NLLVKELLTQ SDHPAVAYIF
SSGQRNVKDD PADYTEYITP TEPENYMSIL NILSHPFSRG SCHIASPDVD VAPILDPRYF
SHPADIEIMA RSAMFVEKLA STEPFRSTVF QPRGRRLPDG IVPNDLDCAR EFVRRQTISI
MHLSATCSML PREQGGVVDS RLLVYGTRNL RVVDASIFPL EPLGNIQTTV YAVAEKAADM
IRQDRSMIYR QNKL
//