ID A0A0B5DSG6_9ACTN Unreviewed; 320 AA.
AC A0A0B5DSG6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Amino acid oxidase {ECO:0000313|EMBL:AJE43536.1};
DE SubName: Full=D-amino-acid oxidase {ECO:0000313|EMBL:MBB4795010.1};
DE EC=1.4.3.3 {ECO:0000313|EMBL:MBB4795010.1};
DE SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:QEV42040.1};
GN ORFNames=BJY54_005622 {ECO:0000313|EMBL:MBB4795010.1}, CP978_28850
GN {ECO:0000313|EMBL:QEV42040.1}, SNOD_28585
GN {ECO:0000313|EMBL:AJE43536.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE43536.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE43536.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE43536.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV42040.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV42040.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MBB4795010.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4795010.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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; CP009313; AJE43536.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4795010.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV42040.1; -; Genomic_DNA.
DR RefSeq; WP_043445636.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_28585; -.
DR KEGG; snq:CP978_28850; -.
DR HOGENOM; CLU_034311_0_0_11; -.
DR OrthoDB; 246701at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:MBB4795010.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..315
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT BINDING 44..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 298..303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ SEQUENCE 320 AA; 34182 MW; 7EB1E45E7C2D6D0D CRC64;
MDTEQNADVI VVGGGVIGLT TAIVLAERGR KVRVWTREPV ERTTSAVAGA LWWPYRIEPE
ALVGAWALES LLVYEELAER PEETGVRLVE GVHGEASLEE LGSWAAGVGG LRASTRAEYS
GSGLWARLPL IDMSVHLPWL RERLLRAGGR VEERTVVDLA EPGAEAPVVV NCTGLGAREL
VPDPLVHPVR GQLVVVENPG VTTWLTSVAH SSEESTYFFP QPGGLILGGT AQEDDWSLTP
DPRTAEAIVA RCAALRPEIA GARVLEHRVG LRPARPSVRL EREAPTGGGT VVHHYGHGGA
GVTVAWGCAR EAAELAQPDL
//
