NADB_AQUAE
ID NADB_AQUAE Reviewed; 510 AA.
AC O66973;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=L-aspartate oxidase {ECO:0000250|UniProtKB:P10902};
DE Short=LASPO {ECO:0000250|UniProtKB:P10902};
DE EC=1.4.3.16 {ECO:0000250|UniProtKB:P10902};
DE AltName: Full=Quinolinate synthase B;
GN Name=nadB; OrderedLocusNames=aq_777;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06932.1; -; Genomic_DNA.
DR PIR; B70368; B70368.
DR RefSeq; NP_213534.1; NC_000918.1.
DR RefSeq; WP_010880472.1; NC_000918.1.
DR AlphaFoldDB; O66973; -.
DR SMR; O66973; -.
DR STRING; 224324.aq_777; -.
DR PRIDE; O66973; -.
DR EnsemblBacteria; AAC06932; AAC06932; aq_777.
DR KEGG; aae:aq_777; -.
DR PATRIC; fig|224324.8.peg.618; -.
DR eggNOG; COG0029; Bacteria.
DR HOGENOM; CLU_014312_3_2_0; -.
DR InParanoid; O66973; -.
DR OMA; HCVQWLI; -.
DR OrthoDB; 153138at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IBA:GO_Central.
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:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..510
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184378"
FT ACT_SITE 271
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 24..27
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 213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 356
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 372..373
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 510 AA; 57793 MW; B6D5AD83438D0C42 CRC64;
MNYFLRFDTS LLPEEEAKVL ICGSGIGGLA TAISLKELGI EPLILTRGIG NTYYSQGGIA
AAVLPDDSPY LHYCDTLRAG RYLNHELHTK LLTYEGIFRI LDLERWGVDF DKKNGFYETT
LEGGHSKPRV LKVKDYTGRE IYTKLLKKTE ELGIKILHGE LQEIIIEENG VQGVIYSEEG
SLKFIRTPLL ILATGGAASM YYYTSNPKKV RGDAIGIAFR MGATVKNPEF VQFHPTVLKG
TNLLISEAVR GEGAILVNDR GERFVNELLP RDEVARAIYN QIKRGREVYL DLRPVAQKGI
KIEERFPTIY SFLRERGYDP YREPVPIIPA AHYYIGGIEV DDRGRTSIQG LYAVGECSCT
GIHGANRLAS NSLLEGVVFG HRTAYQVYLD LKILKPSKVN FRSERAGSDK PNLGIEELKK
LMWNYVGLER DEEGLTYVKK RILSVLSQAK HWEPTPQNRQ LYDILLVALC TVEGALMRKE
SRGVHYRKDY PTEREVYRRD TIITRDLFEL
