ID A0A1W2TS19_ROSNE Unreviewed; 639 AA.
AC A0A1W2TS19;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative GMC oxidoreductase-like protein {ECO:0000313|EMBL:GAP91305.2};
GN ORFNames=SAMD00023353_6000710 {ECO:0000313|EMBL:GAP91305.2};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP91305.2};
RN [1] {ECO:0000313|EMBL:GAP91305.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP91305.2};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; DF977505; GAP91305.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2TS19; -.
DR STRING; 77044.A0A1W2TS19; -.
DR OMA; IYAGWPR; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000054516; 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:SF115; DEHYDROGENASE XPTC-RELATED; 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.
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:UP000054516};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..639
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012687122"
FT DOMAIN 314..328
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 56..57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 565
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 639 AA; 69410 MW; CCA5F59663BEA25B CRC64;
MLPSFVVSAA LWAISLLEAA YALGEVNSQY GSHIRSSYVV SNVKSSYDYV IVGAGTSGLT
VADRLSADGK SSVLVIENGK VVDSPRISQV YSGLAAIGST WSYQINSVRQ PNLNNRSTAI
TVGKLVGGSS AINAMMTIRG TSDDYDRWGS FFGQDSSWSW AGLLPYFKKA LSFSPPDGEV
AKSVNITWDT SYWGNSSSVH TSWPHFQWPA LEAQFEAFRD IPGVEFPPDS GSGKAGVYWF
PTFMDPEKVE RSYARTGHFD NINRTNFEVV TDSKVTKILL DDGVAIGVSF ERKTDNSTSI
VTVKADKEVI VAAGAIHSPQ LLQQSGIGPR ALLEAAGIDT AVDLPGVGQN FQDHPMVFTS
VTLQNFTMHP NPTDMYSNQS FLAWAQELWR VNKTGPYSLG VGNAAAWLSM PVIAPDTFEG
IASKLEGLDH AALLPNGTHP TIVAGYKAQM KDMAAAIRSP DTAFYNHVLT GGASSGTIVD
LHPLSRGTVN INTADPFGSE PVVDYRALTN PVDLDIMVEI LRFTRRYYFE TRMRGFAPRQ
VQPAESVREP EALKAFLRQN VNPSYFHPVG TCSMLPRELG GVVDEQLKVY GVKRLRVVDA
SIMSVLVGAN TCQTTYAIAE KAADLIKADD HGDWTRVTG
//
