ID A0A1V6RZY2_9EURO Unreviewed; 363 AA.
AC A0A1V6RZY2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN ORFNames=PENVUL_c014G08817 {ECO:0000313|EMBL:OQE07352.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE07352.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE07352.1}.
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DR EMBL; MDYP01000014; OQE07352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RZY2; -.
DR STRING; 29845.A0A1V6RZY2; -.
DR OrthoDB; 1385925at2759; -.
DR Proteomes; UP000191518; 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:UP000191518}.
FT DOMAIN 5..344
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 196
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 363 AA; 39401 MW; 72DD3A18FD9D0E10 CRC64;
MANNIVVLGA GVSGLTTAYL LSQDPANKIT VLAKHMPGDY DIEYASPWAG ANYMPVGKEG
SAHQKWERDT WPVLKEIADK YPEAGIHFRG SFIYNRKKDQ GSETGRSFSE LVQPNPWYKD
VVLDFKSVPS DQLLPGINNG QEFTSVCINT AIYLPWLVGQ CLKNGAVFKR AVFKHIADAA
NAHHTGQKAD VVVNCTGLSS KTLGGVLDDK MYPARGQIVV VRNDPGPMMS TSGTDDGEDE
LLYIMTRAAG GGTILGGSYQ KNNWDAIPDM NLANRIMKRC IEVCPNLVKK GQGIEGLDIV
RHGVGLRPLR EGGTRIEKDK VGGVAIVHNY GHGGFGYQAS FGCSYSAVSL VNEILQNKSR
AKL
//
