ID Q57L60_SALCH Unreviewed; 540 AA.
AC Q57L60;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00021901, ECO:0000256|RuleBase:RU362049};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173, ECO:0000256|RuleBase:RU362049};
GN Name=nadB {ECO:0000313|EMBL:AAX66552.1};
GN OrderedLocusNames=SCH_2646 {ECO:0000313|EMBL:AAX66552.1};
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314 {ECO:0000313|EMBL:AAX66552.1, ECO:0000313|Proteomes:UP000000538};
RN [1] {ECO:0000313|EMBL:AAX66552.1, ECO:0000313|Proteomes:UP000000538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67 {ECO:0000313|EMBL:AAX66552.1,
RC ECO:0000313|Proteomes:UP000000538};
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.Y., Wang H.S.,
RA Lee Y.S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX66552.1; -; Genomic_DNA.
DR RefSeq; WP_000989182.1; NC_006905.1.
DR AlphaFoldDB; Q57L60; -.
DR KEGG; sec:SCH_2646; -.
DR HOGENOM; CLU_014312_3_0_6; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000000538; 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 PIRSF; PIRSF000171; SDHA_APRA_LASPO; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
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 Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 10..392
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 441..522
FT /note="Fumarate reductase/succinate dehydrogenase
FT flavoprotein-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02910"
FT COILED 453..480
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 290
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000171-1"
SQ SEQUENCE 540 AA; 60150 MW; 35274DD5880E5B77 CRC64;
MMTTPELSCD VLIIGSGAAG LSLALRLAEK HKVIVLSKGP VSEGSTFYAQ GGIAAVFDET
DSIASHVEDT LIAGAGICDR HAVEFVASNA RTCVQWLIDQ GVLFDTHVQP NGKESYHLTR
EGGHSHRRIL HAADATGKEV ETTLVSRAQN HPNIQVLERS NAVDLIISDK MGLPGPRRVV
GAWIWNRNKE WVETCHAKSV VLATGGASKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF
NQFHPTALYH PQARNFLLTE ALRGEGAYLK RPDGSRFMPD VDERGELAPR DIVARAIDHE
MKRLGADCMF LDISHKPDDF VRQHFPMIYA KLLDLGMDLT KEPIPIVPAA HYTCGGVVVD
DYGRTDVDGL YAIGEVSYTG LHGANRMASN SLLECLVYGW SAAMDIDRRM PSVHSVDVLP
ARDESRVENA DERVVIQHNW HELRLLMWDY VGIVRTTKRL ERALRRITML QQEIDEYYAN
FRVSNNLLEL RNLVQVAELI VRCAMMRKES RGLHFTLDYP QQLAESGPSI LSPLTPHINR
//
