NADB_LISIN
ID NADB_LISIN Reviewed; 484 AA.
AC Q929Z2;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=lin2131;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL596171; CAC97361.1; -; Genomic_DNA.
DR PIR; AI1698; AI1698.
DR RefSeq; WP_010991770.1; NC_003212.1.
DR AlphaFoldDB; Q929Z2; -.
DR SMR; Q929Z2; -.
DR STRING; 272626.lin2131; -.
DR EnsemblBacteria; CAC97361; CAC97361; CAC97361.
DR KEGG; lin:nadB; -.
DR eggNOG; COG0029; Bacteria.
DR HOGENOM; CLU_014312_3_2_9; -.
DR OMA; DSPDIHY; -.
DR OrthoDB; 153138at2; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000002513; 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-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; IPR005288; NadB.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR42716; PTHR42716; 1.
DR Pfam; PF00890; FAD_binding_2; 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;
KW Pyridine nucleotide biosynthesis.
FT CHAIN 1..484
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184386"
FT ACT_SITE 270
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 11..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 40..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 203
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 352
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 368..369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT SITE 111
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
SQ SEQUENCE 484 AA; 53411 MW; 548B9BA10EBA4261 CRC64;
MTKERVIIIG SGIAGCTAAL RLMQDYDVTI ITKGHKEQSN SMLAQGGVAA AISKSDTPKK
HFSDTFQAGC FHNKVRAVNQ LVTCGPIVIQ KLINEGMTFD EKDGELSLGL EGAHQLPRIL
HSGGDQTGKF LTTFLQEKLT KVNWQEQKMA IEIIKHDGRA IGVHCLDKEN QLHTYYGEHI
ILASGGLGQL FPVTTNAATI SGDGLALAYR ADATLSDMEF IQFHPTLLFL NGRCHGLISE
AVRGEGATLI RADGSAIMET VHPLADLAPR DVVAATLFEE IERGNQVFLD ITKVAHFEKR
FPAITTSLDE HQVPFRETKR IPVHPGAHFL MGGVRTDLNG KTNIPHLYAI GEVANTGVHG
ANRLASNSLL ETLVFGEKVA EYIHTQKNNR IIAPENPPTY QTTMPHLPEK HILQEKIWET
LGITRKPEKI TEFLHWLETF DYANHTRETA EISHMIITSK LIAESALKRT ESLGAHRILK
GVTK
