NADB_PYRFU
ID NADB_PYRFU Reviewed; 464 AA.
AC Q8TZL4;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=PF1976;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL82100.1; -; Genomic_DNA.
DR RefSeq; WP_011013118.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8TZL4; -.
DR SMR; Q8TZL4; -.
DR IntAct; Q8TZL4; 1.
DR STRING; 186497.PF1976; -.
DR PRIDE; Q8TZL4; -.
DR EnsemblBacteria; AAL82100; AAL82100; PF1976.
DR GeneID; 41713798; -.
DR KEGG; pfu:PF1976; -.
DR PATRIC; fig|186497.12.peg.2049; -.
DR eggNOG; arCOG00572; Archaea.
DR HOGENOM; CLU_014312_3_2_2; -.
DR OMA; HCVQWLI; -.
DR OrthoDB; 8547at2157; -.
DR PhylomeDB; Q8TZL4; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000001013; 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; 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..464
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184409"
FT ACT_SITE 248
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 8..11
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 37..44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 345..346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT SITE 102
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
SQ SEQUENCE 464 AA; 51710 MW; 413C23A61594A7B3 CRC64;
MKVAVVGSGL AGLTAAMSLA KKGIEVTVFG PKPKESNSYL AQAGIAFPIS DGDSIISHVT
DTIRGGKYLN DVTVVWNVIS KSTEAYHFLT SLGIEFTSRE LEGGHSFPRI FTIKNETGKY
IIPVLEKHAK EMGVNFIRKF AEEVAIHNKK IVGVFVEGEL LYFDAVIIAS GGFSGLYKFT
AGNPWNLGIP IGDLALKGVP LRDIEFIQFH PTGFIGKRTY LISEAVRGAG AKLVTGEGER
FVNELETRDV VAREIYRKML EGKGVFLDAT GIEDFKRRFP YIYSFLRREG INPKRDLIPV
TPVAHYTIGG ISVDIFYRTP IKGLYAIGEA ACNGFHGANR LASNSLLECI VSGIEVSRTV
IREKPRGERK EAKYHGYEPG NVDEVRDIMW NHAGIIRREE SLRLGLKKLE KVEADPRVKI
LAEAVLKCAL AREESRGAHY REDYPYSREE FRRPSIFRVE NCML
