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Database: UniProt
Entry: U5Q6K5_9BACT
LinkDB: U5Q6K5_9BACT
Original site: U5Q6K5_9BACT 
ID   U5Q6K5_9BACT            Unreviewed;       525 AA.
AC   U5Q6K5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
DE            EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN   Name=nadB {ECO:0000313|EMBL:AGY52990.1};
GN   ORFNames=BRDCF_p363 {ECO:0000313|EMBL:AGY52990.1};
OS   Bacteroidales bacterium CF.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY52990.1, ECO:0000313|Proteomes:UP000017642};
RN   [1] {ECO:0000313|EMBL:AGY52990.1, ECO:0000313|Proteomes:UP000017642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AGY52990.1};
RX   PubMed=24356833;
RA   Tang S., Edwards E.A.;
RT   "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT   Dechlorinating Enrichment Culture.";
RL   Genome Announc. 1:e01066-13(2013).
CC   -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate.
CC       {ECO:0000256|RuleBase:RU362049}.
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,
CC         ECO:0000256|RuleBase:RU362049};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC       from L-aspartate (oxidase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004950, ECO:0000256|RuleBase:RU362049}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362049}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC       subfamily. {ECO:0000256|ARBA:ARBA00008562,
CC       ECO:0000256|RuleBase:RU362049}.
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DR   EMBL; CP006772; AGY52990.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5Q6K5; -.
DR   STRING; 1400053.BRDCF_p363; -.
DR   KEGG; bacc:BRDCF_p363; -.
DR   HOGENOM; CLU_014312_3_0_10; -.
DR   OrthoDB; 9806724at2; -.
DR   UniPathway; UPA00253; UER00326.
DR   Proteomes; UP000017642; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.20.58.100; Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR005288; NadB.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   NCBIfam; TIGR00551; nadB; 1.
DR   PANTHER; PTHR42716; L-ASPARTATE OXIDASE; 1.
DR   PANTHER; PTHR42716:SF2; L-ASPARTATE OXIDASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF02910; Succ_DH_flav_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF46977; Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362049};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362049};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362049};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|RuleBase:RU362049};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017642}.
FT   DOMAIN          5..375
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          426..511
FT                   /note="Fumarate reductase/succinate dehydrogenase
FT                   flavoprotein-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02910"
SQ   SEQUENCE   525 AA;  58753 MW;  DA8F53D15757D3AF CRC64;
     MHRYDYIIVG SGLAGLYASY RASLYGKVAL ITKTTVRESN SYYAQGGIAA VTDEEDRPAF
     HFDDTVTAGR GLCDYNAVDI LVNEGPHRIV DLVRDGMKFD MLGDSFALGL EGGHHMRRIL
     HAGGDVTGMK ITNFMIEKVL ADKNIILFEN HTVLSIIQET GKCYGVRTWN SETESEEIFM
     GNYTFLASGG ASAIFKRTTN PHTTTGDGIA LAYEADCKIA DMEFVQFHPT ALYTETDKTF
     LISEAVRGEG AQLLNLKGER FMPAIHELAE LAPRDVVARS IFRQILQQDE PYVHLSLKHI
     DPERIKSRFP NIFEKCRQLG IDMTDKIPVA PAAHYMVGGV RSDVNGRTNI ENLYVCGELA
     STGIMGANRL ASNSLLECLV FGYRAVEDTR EISTGKSSNE VITDLKPIYR KDPSKEEMFR
     NLKVKVSNLM NDNAGIIRNE KLLSEGLEIL EKEKEALGND KEEYYTLLSY NLITVAELII
     KPAIYRKESR GGHYREDYPH EENSFIKHII QQKGRPIGAI PVDDK
//
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