ID A0A0G2DU57_9PEZI Unreviewed; 618 AA.
AC A0A0G2DU57;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative gmc oxidoreductase {ECO:0000313|EMBL:KKY14472.1};
GN ORFNames=UCDDS831_g08132 {ECO:0000313|EMBL:KKY14472.1};
OS Diplodia seriata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=420778 {ECO:0000313|EMBL:KKY14472.1, ECO:0000313|Proteomes:UP000034182};
RN [1] {ECO:0000313|EMBL:KKY14472.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY14472.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY14472.1, ECO:0000313|Proteomes:UP000034182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS831 {ECO:0000313|EMBL:KKY14472.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KKY14472.1}.
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DR EMBL; LAQI01000228; KKY14472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2DU57; -.
DR Proteomes; UP000034182; 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:SF138; DEHYDROGENASE PKFF-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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..618
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002543042"
FT DOMAIN 319..333
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 555
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 599
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
SQ SEQUENCE 618 AA; 66234 MW; EB5432191930EC72 CRC64;
MFSLSLLAPL LCAHLVQSVP LAPRSELVAR KLLGSSFGVP RNATYDYVVV GGGNAGLTVA
ARLAEDSSVS VAVIEAGSFY EIENGNLSQI PAYDTMWTGK DPEDTNRVDW GFVTEPQKEL
LDAKVHYARG KTLGGSTARN YMAYHRGTVG TYQKWAEQVG DDSYTFDNFA PFFEKSLNFT
PPKSSRAANA TPEYDEATLG KGDGPLSLTF SNYANAMASW VQKGFAEIGI GWQKGFTSGT
LNGSSYVLEN IDATLQTRES SETAFLQPAL EKTSLMVYQS TLAKKILFDA SKKATGVAVD
SDGVQYTLSA TKEVIVSAGA FQSPQLLMVS GVGPKATLDK FDIPVVADLA GVGQNMWDHV
LMGPSYRVNV MTSSALADPA VLAQAQQDYL ERQEGILTNS GGDFLAWEKI PAAQRAGFDN
ATRGALAAFP ADWPEVEYLS MSGFLGYQQD YARDAPTDGF NYATVSTALV APLSRGSVSI
ASADMADAPL IDPRWLTHPA DRAVVVQGYK RVRQMFAATA MQDVLIGPEY FPGADVQTDD
EILEVIRKTV STVYHAACTC AMGRANDSSA VVDSSARVFG VDGLRVVDAS SFPLLPPGHP
VATIYALAEK IAHDILNP
//