NADB_SALTY
ID NADB_SALTY Reviewed; 540 AA.
AC Q8ZMX9;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=STM2641;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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}.
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DR EMBL; AE006468; AAL21535.1; -; Genomic_DNA.
DR RefSeq; NP_461576.1; NC_003197.2.
DR RefSeq; WP_000989177.1; NC_003197.2.
DR PDB; 5KXJ; X-ray; 1.87 A; A=1-540.
DR PDBsum; 5KXJ; -.
DR AlphaFoldDB; Q8ZMX9; -.
DR SMR; Q8ZMX9; -.
DR STRING; 99287.STM2641; -.
DR PaxDb; Q8ZMX9; -.
DR EnsemblBacteria; AAL21535; AAL21535; STM2641.
DR GeneID; 1254164; -.
DR KEGG; stm:STM2641; -.
DR PATRIC; fig|99287.12.peg.2791; -.
DR HOGENOM; CLU_014312_3_0_6; -.
DR OMA; HCVQWLI; -.
DR PhylomeDB; Q8ZMX9; -.
DR BioCyc; SENT99287:STM2641-MON; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000001014; 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 3D-structure; Cytoplasm; FAD; Flavoprotein; Nucleotide-binding;
KW Oxidoreductase; Pyridine nucleotide biosynthesis; Reference proteome.
FT CHAIN 1..540
FT /note="L-aspartate oxidase"
FT /id="PRO_0000184400"
FT ACT_SITE 290
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 16..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT BINDING 38
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 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 121
FT /note="Important in orienting the L-aspartate substrate"
FT /evidence="ECO:0000250|UniProtKB:P10902"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:5KXJ"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 80..99
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:5KXJ"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 191..202
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 290..304
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 318..324
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:5KXJ"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 344..354
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 390..409
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 430..450
FT /evidence="ECO:0007829|PDB:5KXJ"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 457..477
FT /evidence="ECO:0007829|PDB:5KXJ"
FT HELIX 485..506
FT /evidence="ECO:0007829|PDB:5KXJ"
SQ SEQUENCE 540 AA; 60109 MW; EE678152DB48B769 CRC64;
MMTTPELSCD VLIIGSGAAG LSLALRLAEK HKVIVLSKGP VSEGSTFYAQ GGIAAVFDET
DSIASHVEDT LIAGAGICDR HAVEFVASNA RTCVQWLIDQ GVLFDTHVQP NGKESYHLTR
EGGHSHRRIL HAADATGKEV ETTLVSRAQN HPNIQVLERS NAVDLIISDK MGLPGPRRVV
GAWIWNRNKE WVETCHAKSV VLATGGASKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF
NQFHPTALYH PQARNFLLTE ALRGEGAYLK RPDGSRFMPD VDERGELAPR DIVARAIDHE
MKQLGADCMF LDISHKPDDF VRQHFPMIYA KLLDLGMDLT KEPIPVVPAA HYTCGGVVVD
DYGRTDVDGL YAIGEVSYTG LHGANRMASN SLLECLVYGW SAAMDIDRRM PSVHSVDALP
AWDESRVENA DERVVIQHNW HELRLLMWDY VGIVRTTKRL ERALRRITML QQEIDEYYAN
FRVSNNLLEL RNLVQVAELI VRCAMMRKES RGLHFTLDYP QQLAESGPSI LSPLTPHINR
