ID A0A2S4LAQ4_9HYPO Unreviewed; 355 AA.
AC A0A2S4LAQ4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE SubName: Full=D-amino-acid oxidase {ECO:0000313|EMBL:POR39507.1};
GN ORFNames=TPAR_00305 {ECO:0000313|EMBL:POR39507.1};
OS Tolypocladium paradoxum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=94208 {ECO:0000313|EMBL:POR39507.1, ECO:0000313|Proteomes:UP000237481};
RN [1] {ECO:0000313|EMBL:POR39507.1, ECO:0000313|Proteomes:UP000237481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR39507.1,
RC ECO:0000313|Proteomes:UP000237481};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (JAN-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: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:POR39507.1}.
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DR EMBL; PKSG01000034; POR39507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4LAQ4; -.
DR STRING; 94208.A0A2S4LAQ4; -.
DR OrthoDB; 1385925at2759; -.
DR Proteomes; UP000237481; 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; IPR006181; D-amino_acid_oxidase_CS.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF11; D-ASPARTATE OXIDASE; 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.
DR PROSITE; PS00677; DAO; 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:UP000237481}.
FT DOMAIN 9..334
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 50..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 188
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 355 AA; 38391 MW; 4D39C8A2BD99EE64 CRC64;
MAAPTNEAIV IVGAGIIGLD VALVLAERGL GPHTTVIAEY LPGDTSPDYT SPWAGCNFSG
ISGSDKNALR WDRMGYAHLT RLASERGEEA YVARTHSIEY WDADAPHDKI KAMSDYLEDF
KILPAAELPP GVEYGISCTT LTLHAPKHIE YLYASLRDQH GVRFVRKKLD SIRAAFASPR
TKAVFNCTGN AARTLPGVQD AKCYPTRGQV VLARAPAVKH NVMRHGRDYE TYVIPRPGSN
GNVILGGYMQ KGVGNAATYS YETDSIIART TALCPDLREQ PREVLAAFAG MRPSREGGAR
VEREDISVNG ARRALVHNYG AGGTGFQAGY GMAMDAVGTV EDVLRELQAG PRARL
//
