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Database: UniProt
Entry: A0A1I3F1H8_9ACTN
LinkDB: A0A1I3F1H8_9ACTN
Original site: A0A1I3F1H8_9ACTN 
ID   A0A1I3F1H8_9ACTN        Unreviewed;       296 AA.
AC   A0A1I3F1H8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=D-amino-acid oxidase {ECO:0000313|EMBL:SFI05023.1};
GN   ORFNames=SAMN05216561_104179 {ECO:0000313|EMBL:SFI05023.1};
OS   Nocardioides psychrotolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1005945 {ECO:0000313|EMBL:SFI05023.1, ECO:0000313|Proteomes:UP000198649};
RN   [1] {ECO:0000313|EMBL:SFI05023.1, ECO:0000313|Proteomes:UP000198649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.11156 {ECO:0000313|EMBL:SFI05023.1,
RC   ECO:0000313|Proteomes:UP000198649};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOQG01000004; SFI05023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3F1H8; -.
DR   STRING; 1005945.SAMN05216561_104179; -.
DR   OrthoDB; 246701at2; -.
DR   Proteomes; UP000198649; 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: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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000198649}.
FT   DOMAIN          3..294
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         39..40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         277..282
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   296 AA;  31262 MW;  469D5E14B5363175 CRC64;
     MSRVIVVGAG VVGLSCAVRL LEAGHRVDVV ARDLPRETTS AVAAAIWYPY RALPQDRVTA
     WSATTYDELA ALAVDAPQSG VRMVAGTEVV PASVPDPWWV SAVPSLSRVD RGWSFVAPVV
     EMPVYLGWLA ARVEALGGTL TRLSLRVLPD GSDLVVNCSG IGSRLLAADL EVTAVRGQVV
     YVDRQGLGLD QWWLDGAGPT YVVPREHDVV IGGTAEEGDW SRTPSPETAA AILARASLLV
     PELALARVRG HKVGLRPARP GVRLERQGRV VHCYGHGGSG VTLSWGCAAE VAALAS
//
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