ID G1XID7_ARTOA Unreviewed; 357 AA.
AC G1XID7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN ORFNames=AOL_s00097g114 {ECO:0000313|EMBL:EGX47068.1};
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:EGX47068.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX47068.1, 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|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000189-1};
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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:EGX47068.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADOT01000172; EGX47068.1; -; Genomic_DNA.
DR RefSeq; XP_011124249.1; XM_011125947.1.
DR AlphaFoldDB; G1XID7; -.
DR STRING; 756982.G1XID7; -.
DR GeneID; 22895138; -.
DR eggNOG; KOG3923; Eukaryota.
DR HOGENOM; CLU_034311_1_0_1; -.
DR InParanoid; G1XID7; -.
DR OMA; CHGGWKY; -.
DR OrthoDB; 1385925at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF16; D-AMINO ACID OXIDASE (AFU_ORTHOLOGUE AFUA_5G11290); 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT DOMAIN 5..344
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 45..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 357 AA; 38768 MW; 947B3CEE27626C2C CRC64;
MSSAKIVVIG AGVAGLTTAL LLAKSRHSVT VIAKHMPGDY DIEYTSPWAG ANYFPFSIAE
DSSRKWERAT YPELMRLATQ VPESGIHVQD ANIFIVDGIP ITPFMKDLVD DKPWFKGVVQ
GFRKFDKEEL PKGMKSGTTF KSVCINTAIY LPYLVGQCLK YGVVFKRGIV KHIADAADLH
FSGKKADVVV NCSGLLACKL GGVEDKKVIP ARGQIVLVRN EAPGMYTTSA VHDGDDEMLY
IMMRAAGGGT ILGGCYQKGN WSPEIDPNLA NRIMKRCVDV CPELTGGKGV EGLDIIRHGV
GLRPWREGGA RIEKEVINGV RVVHNYGAAG WGYQASYGMS EDTVALVKES LNLSAKL
//
