NADB_PSEAE
ID NADB_PSEAE Reviewed; 538 AA.
AC Q51363; Q51412;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=PA0761;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD1;
RX PubMed=7737518; DOI=10.1016/0378-1119(95)00028-5;
RA DeVries C.A., Hassett D.J., Flynn J.L., Ohman D.E.;
RT "Genetic linkage in Pseudomonas aeruginosa of algT and nadB: mutation in
RT nadB does not affect NAD biosynthesis or alginate production.";
RL Gene 156:63-67(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RC STRAIN=FRD1;
RX PubMed=7961421; DOI=10.1128/jb.176.21.6677-6687.1994;
RA Devries C.A., Ohman D.E.;
RT "Mucoid-to-nonmucoid conversion in alginate-producing Pseudomonas
RT aeruginosa often results from spontaneous mutations in algT, encoding a
RT putative alternate sigma factor, and shows evidence for autoregulation.";
RL J. Bacteriol. 176:6677-6687(1994).
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; U17232; AAA92356.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04150.1; -; Genomic_DNA.
DR EMBL; L36379; AAA64438.1; -; Genomic_DNA.
DR PIR; T46863; T46863.
DR RefSeq; NP_249452.1; NC_002516.2.
DR RefSeq; WP_003114182.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; Q51363; -.
DR SMR; Q51363; -.
DR STRING; 287.DR97_1223; -.
DR PaxDb; Q51363; -.
DR PRIDE; Q51363; -.
DR EnsemblBacteria; AAG04150; AAG04150; PA0761.
DR GeneID; 882067; -.
DR KEGG; pae:PA0761; -.
DR PATRIC; fig|208964.12.peg.791; -.
DR PseudoCAP; PA0761; -.
DR HOGENOM; CLU_014312_3_0_6; -.
DR InParanoid; Q51363; -.
DR OMA; HCVQWLI; -.
DR PhylomeDB; Q51363; -.
DR BioCyc; PAER208964:G1FZ6-774-MON; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000002438; 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.
DR TIGRFAMs; TIGR00551; nadB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..538
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184393"
FT ACT_SITE 290
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 14..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 43..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 391..392
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 538 AA; 60005 MW; F2B76A500DA814A1 CRC64;
MSQHYQHDVL VIGSGAAGLS LALTLPEHLR IAVLSKGELS QGSTYWAQGG VAAVLDDTDT
VESHVEDTLV AGGGLCREDA VRFTVEHSRE AIQWLIEQGV PFTRDEQHNH EEGSFEYHLT
REGGHSHRRI IHAADATGAA IFNTLLAQAR RRPNIELLSQ RVAVDLITER KLGLPSKRCL
GAYVLNRESG EVDTFRARFS VLASGGASKV YLYTSNPDGN SGDGIAMAWR AGCRVGNLEF
NQFHPTCLYH PQAKSFLITE ALRGEGALLR LPNGERFMPR FDPRGELAPR DIVARAIDHE
MKRLGIDCVY LDISHKPAEF IKAHFPTVYE RCLDFGIDIT QQPIPVVPAA HYTCGGVLVD
QHGHTDVPGL YAIGETTFTG LHGANRMASN SLLECFVYAR SAAADMLQRL PGTPVPESLP
SWDASQVTDS DEDVIIAHNW DELRRFMWDY VGIVRTNKRL QRAQHRVRLL LSEIDEFYSN
YKVSRDLIEL RNLALVAELI IRSAMQRRES RGLHYTLDYP DLLPEARDTI LVPPIYGD
