ID G1XGG2_ARTOA Unreviewed; 615 AA.
AC G1XGG2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=AOL_s00083g93 {ECO:0000313|EMBL:EGX47585.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX47585.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX47585.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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, 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:EGX47585.1}.
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DR EMBL; ADOT01000151; EGX47585.1; -; Genomic_DNA.
DR RefSeq; XP_011123574.1; XM_011125272.1.
DR AlphaFoldDB; G1XGG2; -.
DR STRING; 756982.G1XGG2; -.
DR GeneID; 22894976; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_2_1; -.
DR InParanoid; G1XGG2; -.
DR OMA; NFQVVAF; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000008784; 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:SF210; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00610)-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|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..615
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003427670"
FT DOMAIN 103..126
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 294..308
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 615 AA; 66009 MW; 59723A954E8FA50E CRC64;
MHVSSLLTTS WVAFAVCVAS QATSFDYIIA GGGTAGLVLA ARLTENPDIT VAVIEAGENR
LGDLTILAPG LLTALYTDPN YDWDFHTVPQ TNVNNKVYAQ PRGKVLGGSS AINFLFWTHP
SQKDINNWGT LGNANWTWNA LKPYFKKSEQ YVAPSPQVES DLQTQYIVPG SHGNSGPVKT
GFPDWYSELT EAWPRTFANR GLAVNGDPKD GLALGGYTNL LNLDLSSHTR SYAATAYYAP
NAARPNLSLF TGSLVKKVVT TSVGSQIIAT GIQFIKDGTT TTLTATKEVI VSAGAYGSPQ
ILELSGIGKP SLLNQHGIPV VVNNPNVGEN LQDHVYVPLG FEVNPGIFTL DSFRDQPVFD
AAFQEYLVNQ TGPISVSGAS SALLSLRQIA GNNYNPSTST AASTASSLIG LGLQHALQYQ
DLSTEAVAQE LTLGAGITPI WQNNTKKLFG NELEGNYLSL LGVLEHPFSR GSSHIKSSDP
AVYPAINPNY LSHPLDIEIL SKIVLHLQTI ATTAPLSDLL KGNGTVYQEG YHKITPANVK
AWVKTALQSE FHPSGTCSML PKALGGVVDE RFKVHGVKKL RVVDASVFPL LVRANIQSLV
YAVAERAADF IKEDQ
//