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Database: UniProt
Entry: A0A142YFL2_9PLAN
LinkDB: A0A142YFL2_9PLAN
Original site: A0A142YFL2_9PLAN 
ID   A0A142YFL2_9PLAN        Unreviewed;       112 AA.
AC   A0A142YFL2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=L-aspartate oxidase {ECO:0000313|EMBL:AMV37620.1};
DE            EC=1.4.3.16 {ECO:0000313|EMBL:AMV37620.1};
GN   Name=nadB_2 {ECO:0000313|EMBL:AMV37620.1};
GN   ORFNames=VT85_09295 {ECO:0000313|EMBL:AMV37620.1};
OS   Planctomyces sp. SH-PL62.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctomyces.
OX   NCBI_TaxID=1636152 {ECO:0000313|EMBL:AMV37620.1, ECO:0000313|Proteomes:UP000076365};
RN   [1] {ECO:0000313|EMBL:AMV37620.1, ECO:0000313|Proteomes:UP000076365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL62 {ECO:0000313|EMBL:AMV37620.1,
RC   ECO:0000313|Proteomes:UP000076365};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate + O2 = H2O2 + iminosuccinate;
CC         Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00029281};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC         Evidence={ECO:0000256|ARBA:ARBA00029281};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP011273; AMV37620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142YFL2; -.
DR   STRING; 1636152.VT85_09295; -.
DR   KEGG; plh:VT85_09295; -.
DR   PATRIC; fig|1636152.3.peg.2123; -.
DR   Proteomes; UP000076365; Chromosome.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR005288; NadB.
DR   PANTHER; PTHR42716; L-ASPARTATE OXIDASE; 1.
DR   PANTHER; PTHR42716:SF2; L-ASPARTATE OXIDASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AMV37620.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076365}.
FT   DOMAIN          26..108
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   112 AA;  11705 MW;  66DDCDCCCF81817D CRC64;
     MTTPLLLPRR YLVGFDPREL PHHFADVVVV GGGIAGLRAA LGVPASARVL VVTKDEVRES
     NSSYAQGGIA GVMDPEDRVE DHIADTLSAG KDLCDPSVVD LVVREAPSGS AS
//
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