NADB_BACSU
ID NADB_BACSU Reviewed; 531 AA.
AC P38032;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=L-aspartate oxidase {ECO:0000303|PubMed:8444804};
DE Short=LASPO {ECO:0000305};
DE EC=1.4.3.16 {ECO:0000269|PubMed:18959769};
DE AltName: Full=L-aspartate:fumarate oxidoreductase {ECO:0000303|PubMed:18959769};
DE EC=1.5.99.- {ECO:0000269|PubMed:18959769};
DE AltName: Full=Quinolinate synthase B;
GN Name=nadB {ECO:0000303|PubMed:8444804}; OrderedLocusNames=BSU27870;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=8444804; DOI=10.1128/jb.175.5.1423-1432.1993;
RA Sun D., Setlow P.L.;
RT "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis nadB
RT gene and a nifS-like gene, both of which are essential for NAD
RT biosynthesis.";
RL J. Bacteriol. 175:1423-1432(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBUNIT.
RX PubMed=18959769; DOI=10.1111/j.1742-4658.2008.06641.x;
RA Marinoni I., Nonnis S., Monteferrante C., Heathcote P., Haertig E.,
RA Boettger L.H., Trautwein A.X., Negri A., Albertini A.M., Tedeschi G.;
RT "Characterization of L-aspartate oxidase and quinolinate synthase from
RT Bacillus subtilis.";
RL FEBS J. 275:5090-5107(2008).
CC -!- FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the
CC first step in the de novo biosynthesis of NAD(+) (PubMed:18959769). Can
CC use either oxygen or fumarate as electron acceptors, which allows the
CC enzyme to be functional under aerobic and anaerobic conditions
CC (PubMed:18959769). {ECO:0000269|PubMed:18959769}.
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:0000269|PubMed:18959769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC Evidence={ECO:0000269|PubMed:18959769};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=fumarate + L-aspartate = iminosuccinate + succinate;
CC Xref=Rhea:RHEA:30043, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:77875;
CC Evidence={ECO:0000269|PubMed:18959769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30044;
CC Evidence={ECO:0000269|PubMed:18959769};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:18959769};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P10902};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for L-aspartate (for L-aspartate:oxygen oxidoreductase
CC activity) {ECO:0000269|PubMed:18959769};
CC KM=20.0 mM for L-aspartate (for L-aspartate:fumarate oxidoreductase
CC activity) {ECO:0000269|PubMed:18959769};
CC KM=1.6 mM for fumarate (for fumarate reductase activity)
CC {ECO:0000269|PubMed:18959769};
CC KM=1.43 mM for fumarate (for L-aspartate:fumarate oxidoreductase
CC activity) {ECO:0000269|PubMed:18959769};
CC Note=kcat is 0.18 sec(-1) for L-aspartate:oxygen oxidoreductase
CC activity. kcat is 15.4 sec(-1) for fumarate reductase activity. kcat
CC is 0.50 sec(-1) for L-aspartate:fumarate oxidoreductase activity.
CC {ECO:0000269|PubMed:18959769};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000269|PubMed:18959769, ECO:0000305|PubMed:8444804}.
CC -!- SUBUNIT: Monomer. Homodimer. {ECO:0000269|PubMed:18959769}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expression is repressed in the presence of nicotinic acid.
CC {ECO:0000269|PubMed:8444804}.
CC -!- DISRUPTION PHENOTYPE: Mutant requires exogenous nicotinic acid for
CC growth. {ECO:0000269|PubMed:8444804}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000305}.
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DR EMBL; M98822; AAA21614.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14747.1; -; Genomic_DNA.
DR PIR; C47071; C47071.
DR RefSeq; NP_390665.1; NC_000964.3.
DR RefSeq; WP_003229687.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P38032; -.
DR SMR; P38032; -.
DR STRING; 224308.BSU27870; -.
DR PaxDb; P38032; -.
DR PRIDE; P38032; -.
DR EnsemblBacteria; CAB14747; CAB14747; BSU_27870.
DR GeneID; 938051; -.
DR KEGG; bsu:BSU27870; -.
DR PATRIC; fig|224308.179.peg.3028; -.
DR eggNOG; COG0029; Bacteria.
DR InParanoid; P38032; -.
DR OMA; HCVQWLI; -.
DR PhylomeDB; P38032; -.
DR BioCyc; BSUB:BSU27870-MON; -.
DR BRENDA; 1.4.3.16; 658.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000001570; 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 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Oxidoreductase;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..531
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184380"
FT ACT_SITE 272
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 151..152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 205
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 353
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 369..370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT SITE 112
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
SQ SEQUENCE 531 AA; 58239 MW; AF592AC55EC51259 CRC64;
MSKKTIAVIG SGAAALSLAA AFPPSYEVTV ITKKSVKNSN SVYAQGGIAA AYAKDDSIEA
HLEDTLYAGC GHNNLAIVAD VLHDGKMMVQ SLLERGFPFD RNERGGVCLG REGAHSYNRI
FHAGGDATGR LLIDYLLKRI NSKIKLIENE TAADLLIEDG RCIGVMTKDS KGRLKVRHAD
EVVLAAGGCG NLFLHHTNDL TVTGDGLSLA YRAGAELTDL EFTQFHPTLL VKNGVSYGLV
SEAVRGEGGC LVDENGRRIM AERHPLGDLA PRDIVSRVIH EEMAKGNRVY IDFSAISDFE
TRFPTITAIC EKAGIDIHSG KIPVAPGMHF LMGGVSVNRW GETTVPGLYA IGETACSGLH
GANRLASNSL LEALVFGKRA AEHIIQKPVY NRQYQSGLET SVFYEVPDIE GHELQSKMTS
HMSILREQSS LIELSIWLHT LPFQEVNVKD ITIRQMELSH LWQTAKLMTF SALLREESRG
AHFRTDFPHA EVSWQGRQIV HTKKGTKIRK NEGIWNNESF TAEKITESLF S
