NADB2_RALSO
ID NADB2_RALSO Reviewed; 536 AA.
AC Q8XQG4;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=L-aspartate oxidase 2 {ECO:0000250|UniProtKB:P10902};
DE Short=LASPO 2 {ECO:0000250|UniProtKB:P10902};
DE EC=1.4.3.16 {ECO:0000250|UniProtKB:P10902};
DE AltName: Full=Quinolinate synthase B 2;
GN Name=nadB2; OrderedLocusNames=RSp1263; ORFNames=RS05308;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG Plasmid megaplasmid Rsp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the
CC first step in the de novo biosynthesis of NAD(+).
CC {ECO:0000250|UniProtKB:P10902}.
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:0000250|UniProtKB:P10902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC Evidence={ECO:0000250|UniProtKB:P10902};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P10902};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P10902};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000250|UniProtKB:P10902}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10902}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000305}.
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DR EMBL; AL646053; CAD18414.1; -; Genomic_DNA.
DR RefSeq; WP_011004545.1; NC_003296.1.
DR AlphaFoldDB; Q8XQG4; -.
DR SMR; Q8XQG4; -.
DR STRING; 267608.RSp1263; -.
DR EnsemblBacteria; CAD18414; CAD18414; RSp1263.
DR GeneID; 60504171; -.
DR KEGG; rso:RSp1263; -.
DR PATRIC; fig|267608.8.peg.4755; -.
DR eggNOG; COG0029; Bacteria.
DR HOGENOM; CLU_014312_3_0_4; -.
DR OMA; DSPDIHY; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 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 PANTHER; PTHR42716; PTHR42716; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR00551; nadB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase; Plasmid;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..536
FT /note="L-aspartate oxidase 2"
FT /id="PRO_0000184395"
FT ACT_SITE 284
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 22..25
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 51..58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 385..386
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT SITE 122
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
SQ SEQUENCE 536 AA; 57653 MW; BDF545C8A33E82E7 CRC64;
MTSGQSKHEI RDMKFDVLVV GEGLAALTLL LHLPPSLKIG VISRNKYDEP SSYWAQGGIS
AVFSTDDDHD KHIRDTLLAG DGLCDEAAVR QIVCEGGDVL RWLIDQGVPF TREDGEIHLT
REGGHSERRV AHVDDMTGRG IMRALQAKVA QLPNVIWIRQ YEAVELLSDG QAVSGVIAES
LADGEVTVFS APTVVLAAGG LTGLYQYATN PHASKGEAIA MAWRAGATIE NLEFVQFHPT
AFQIEGRVIS LITEAVRGEG GLLYNVANER FMPGYSSQQE LAPRDVVARA IYSEMQAHGT
SHVWLDITHQ GTAFVEQHFP NLVEITRAHG CDLSQHRVPV SPAAHYTCGG IGADVAGRTN
IEGLYAIGEV ANCGLHGANR LASNSLLECV VMGKACAQSV TDTAGSASRL RLTLPERIET
PFHPNLLADL RAILWNHAGI VRSNTGLEIG LQNMAQLQER HASVLPYGQA LRAQNIFDAA
HLVLLSAAAR KESRGGHFNK DHADKAEAQT TQIPGVPVNF WAAGENASHA AQLAAA
