NADB_HALSA
ID NADB_HALSA Reviewed; 509 AA.
AC Q9HNZ0;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, 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=VNG_1883G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG20080.1; -; Genomic_DNA.
DR PIR; D84339; D84339.
DR RefSeq; WP_010903379.1; NC_002607.1.
DR AlphaFoldDB; Q9HNZ0; -.
DR SMR; Q9HNZ0; -.
DR STRING; 64091.VNG_1883G; -.
DR PaxDb; Q9HNZ0; -.
DR EnsemblBacteria; AAG20080; AAG20080; VNG_1883G.
DR GeneID; 5954007; -.
DR KEGG; hal:VNG_1883G; -.
DR PATRIC; fig|64091.14.peg.1438; -.
DR HOGENOM; CLU_014312_3_2_2; -.
DR InParanoid; Q9HNZ0; -.
DR OMA; HCVQWLI; -.
DR OrthoDB; 8547at2157; -.
DR PhylomeDB; Q9HNZ0; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000000554; 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.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..509
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184407"
FT REGION 389..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
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 45..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 358
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 374..375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT SITE 114
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
SQ SEQUENCE 509 AA; 53226 MW; 2932FA3AB128F10E CRC64;
MTDATTTDVL VLGSGIAGCG AALAAAREGA SVLVATKAQQ PADASTDWAQ GGIATTRDDP
ESLKRDILAA GDGEADPEAV DALVGDAAAA VEDVLVDTLG VPFDGEEGFD YAREAAHSAA
RILHVDAATG HHILGPFLRH LDAHENVDML EDAAALDLIT DEGAVTGALL DRNPRTGDRA
ETGVPVFAGS TVLATGGIGD LYRRSTNPRG STGDGVAMAA LAGADVTDAE YVQFHPTAYD
DADPFLVSEA VRGEGALLRN ADGERFMPDY HEDAELAPRD VVARAVAAER DATGEVRLDV
SPLAFAEEFP GLAEACADRG VDWETGIPVA PCEHFLCGGV AVDTVGRTSL DRLFAVGECA
RTGVHGANRL ASTSLLEGLV WGLRAGETAA GDDRAPAPSE PPELRDRDPD LPDGFAAEKF
RRLRRVMDEH VGLRRTGADL QRAQGVLRRL KGEVDSYART RTSRDLYQLR NAAVVGLLIA
RAAGENPESA GCHHRSDEAA AEEAPDAGH
