ID A0A2J8EGK7_VERDA Unreviewed; 597 AA.
AC A0A2J8EGK7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=BJF96_g6772 {ECO:0000313|EMBL:PNH29933.1}, VDGE_05040
GN {ECO:0000313|EMBL:RXG44435.1};
OS Verticillium dahliae (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=27337 {ECO:0000313|EMBL:RXG44435.1, ECO:0000313|Proteomes:UP000288725};
RN [1] {ECO:0000313|EMBL:PNH29933.1, ECO:0000313|Proteomes:UP000236305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12008 {ECO:0000313|EMBL:PNH29933.1,
RC ECO:0000313|Proteomes:UP000236305};
RA Fan R., Armitage A.D., Cascant-Lopez E., Sobczyk M., Cockerton H.M.,
RA Harrison R.J.;
RT "Comparative genomics yields insights into virulence evolution of
RT Verticillium dahliae.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RXG44435.1, ECO:0000313|Proteomes:UP000288725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Getta Getta {ECO:0000313|EMBL:RXG44435.1,
RC ECO:0000313|Proteomes:UP000288725};
RA Gardiner D.M.;
RT "Genome of Verticillium dahliae isolate Getta Getta.";
RL Submitted (DEC-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, ECO:0000256|RuleBase:RU003968}.
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:RXG44435.1}.
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DR EMBL; MPSH01000023; PNH29933.1; -; Genomic_DNA.
DR EMBL; RSDZ01000082; RXG44435.1; -; Genomic_DNA.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000236305; Unassembled WGS sequence.
DR Proteomes; UP000288725; Chromosome 4.
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; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027424; Glucose_Oxidase_domain_2.
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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000288725};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..597
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040582187"
FT DOMAIN 110..133
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 303..317
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 52..53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 112
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 120..123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 568
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 597 AA; 64875 MW; FF25A2A8FE2921FD CRC64;
MPSIKAVILA CLAAASQLAS SWPTASMDGI NILSRQNQVQ NEYDYIIVGG GTSGLTVGNR
LTENNSGVSV LVVEYGYYDN QSGMNPRRMF NLTSRPQQNL NGRSFSVGIG CVVGGSSNVN
GQVFLRGTSE EYNAWAELGG PGSTWNWEGL LPYFRKGITL TGPNPQHAQE FNIKWDMQYW
GTTSKIYATF GRDAPTQLMK VLYNAMAAMP GMTVPVDSGA GQAGLYWYPM SMDPTNFQRS
YSRTGHWHGI SRPNYQMVVG AKVNRILWGA DNTATGIQFV SRNQTGGPAT QVRARREVLL
AAGTVHTPQV LMLSGVGPQA LLQQARIPVR VDLPGVGSNF QDHSYIPSIA YQWGTTPGGG
GGFPGFPTQG GAPALAAMIG LPVVSPQRYQ QLATRYESQN PTSHLPSSYT AEQIAGYRKQ
QEIYARLMRS TNVVFLEMMM FGPGGSVQNL HPHSRGTILI NPSNPEGDMI IDYRAATNDV
DLEVMIETIK FMRRYMTTGQ LAQYNARETS PGTGVSSDQQ LIQWARGQVI PSVYHPVGTC
SKQPREHGGV VDENLRVHGT KNLRVIDGSI MPTIVGATTS MAVYAIAEKA ADLIKTT
//
