NADB_SACS2
ID NADB_SACS2 Reviewed; 472 AA.
AC Q97ZC5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
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=SSO0997;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK41268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK41268.1; ALT_INIT; Genomic_DNA.
DR PIR; E90251; E90251.
DR RefSeq; WP_009989244.1; NC_002754.1.
DR AlphaFoldDB; Q97ZC5; -.
DR SMR; Q97ZC5; -.
DR STRING; 273057.SSO0997; -.
DR EnsemblBacteria; AAK41268; AAK41268; SSO0997.
DR GeneID; 44129928; -.
DR KEGG; sso:SSO0997; -.
DR PATRIC; fig|273057.12.peg.994; -.
DR eggNOG; arCOG00572; Archaea.
DR HOGENOM; CLU_014312_3_2_2; -.
DR InParanoid; Q97ZC5; -.
DR OMA; HCVQWLI; -.
DR PhylomeDB; Q97ZC5; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000001974; 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..472
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184411"
FT ACT_SITE 256
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 7..10
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 36..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 332
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 348..349
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 472 AA; 52645 MW; DABAE606463C353D CRC64;
MIYIFGSGLA GLSAAISLHK SGYKVTIISK KINGGSSYWA KGGIAAAVGN DDSPELHKID
TLEVGDGLCD SKTVDYVTRE IRYVVSTVEK WGFKFDDDLR LEGGHSKRRI LHKTDDTGRE
ITNFLLNLAK KKGINLIEDK LLALKVKDGK VAGFITEKGG SFDAEKVVLA TGGYGYLFKF
TSNPSTNIGD GIAIAFKAGA LVSDTEFVQF HPTVTTFDGQ AYLLTETLRG EGAILVNERN
ERFVFKYDSR GELAPRDVLS RAIYDQYKKG HTVYIDLSPI EDFDRKFPIL SNYVKRYGKR
LQVFPGVHYT IGGIRVNTRG ESNIKGLYAI GEVTDTGLHG ANRLASNSLA EDLVYGVNLV
RYIDNWEGLS IDDVKEVIEV RLRNSSNRLS LEEIREYNWN YLGIVRNGEG LDKLVKIYES
NDTFNDNASL VSLLSAKGAL LRTESRGAHY REDYPNKSWE DGKRIYFMVS RN
