ID   NADA_BACC3              Reviewed;         368 AA.
AC   C1ETM6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00569};
DE            EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00569};
GN   Name=nadA {ECO:0000255|HAMAP-Rule:MF_00569}; OrderedLocusNames=BCA_4541;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC       Rule:MF_00569}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O +
CC         phosphate + quinolinate; Xref=Rhea:RHEA:25888, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29959, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:77875; EC=2.5.1.72;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00569};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00569};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00569};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00569};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00569}.
CC   -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 3
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00569}.
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DR   EMBL; CP001407; ACO30773.1; -; Genomic_DNA.
DR   RefSeq; WP_000025291.1; NZ_CP009318.1.
DR   AlphaFoldDB; C1ETM6; -.
DR   SMR; C1ETM6; -.
DR   EnsemblBacteria; ACO30773; ACO30773; BCA_4541.
DR   KEGG; bcx:BCA_4541; -.
DR   PATRIC; fig|572264.18.peg.4490; -.
DR   OMA; CFCSTMN; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000002210; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008987; F:quinolinate synthetase A activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10800; -; 3.
DR   HAMAP; MF_00569; NadA_type3; 1.
DR   InterPro; IPR003473; NadA.
DR   InterPro; IPR036094; NadA_sf.
DR   InterPro; IPR023515; Quinolinate_synth_A_type3.
DR   PANTHER; PTHR30573; PTHR30573; 1.
DR   Pfam; PF02445; NadA; 1.
DR   SUPFAM; SSF142754; SSF142754; 1.
DR   TIGRFAMs; TIGR00550; nadA; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN           1..368
FT                   /note="Quinolinate synthase"
FT                   /id="PRO_1000146822"
FT   BINDING         46
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         63
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         110
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         141..143
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         162
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         230
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         256..258
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         273
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         320
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
SQ   SEQUENCE   368 AA;  41651 MW;  4757F2A7D00FCAFE CRC64;
     MSILEKVQPI ETMLPERYYT MSTEDMEKRV REIKEKMGET LFIPGHHYQK DEVVQFSDAA
     GDSLQLAQVA ASNKEAKYIV FCGVHFMAET ADMLTTDEQV VILPDMRAGC SMADMADIEQ
     TERAWKELTK LFGDTMIPLT YVNSTAAIKA FCGRNGGATV TSSNAKQMVS WAFTQKERLV
     FLPDQHLGRN TAYDLGIPLD KMAVWDPHTD SLEYDGDIEE IQVILWKGHC SVHQNFTVKN
     IENVRKNHPD MNIIVHPECC YEVVAASDYA GSTKYIIDMI ELAPSGSKWA IGTEMNLVNR
     IIQQHPDKEI VSLNPFMCPC LTMNRIDLPH LLWALETIER GEEINVISVD KQVTEEAVLA
     LNRMLERV