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Database: UniProt
Entry: G1XGG2_ARTOA
LinkDB: G1XGG2_ARTOA
Original site: G1XGG2_ARTOA 
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
//
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