ID   NADA_HALS3              Reviewed;         374 AA.
AC   B0R6K3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=OE_3644F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP14372.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0R6K3; -.
DR   SMR; B0R6K3; -.
DR   EnsemblBacteria; CAP14372; CAP14372; OE_3644F.
DR   KEGG; hsl:OE_3644F; -.
DR   HOGENOM; CLU_047382_2_0_2; -.
DR   OMA; CFCSTMN; -.
DR   PhylomeDB; B0R6K3; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000001321; 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..374
FT                   /note="Quinolinate synthase"
FT                   /id="PRO_1000129456"
FT   BINDING         53
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         70
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         116
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         148..150
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         169
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         236
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         262..264
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         279
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         327
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
SQ   SEQUENCE   374 AA;  41306 MW;  A52B4985169498B2 CRC64;
     MDTSSFETDL SLFKYDDLEA LPDEYRELTP TARTERIEAA RAELGDDVVV LGHNYQRREI
     VEHADFVGDS YQLSKEAANA DADYVIFGGV TFMAESADII TDDSQSVILP SMEASCPMAG
     MAEALQVDAA WADITAAAPD ETIIPITYMN SYADLKAFCA EQGGLVCTSS NAHRAFEWAF
     ERGDKVLFLP DKHLGENTAH RLGMADATVE WDPWAAEGKT AEEVADADIV LWDGYCQVHE
     RFTPEHVAEV RADHEDANVV VHPECRREVV EAADVVGSTA TITETVADAD PGETWAIGTE
     IHLANHLQRW HPEVNVVPLC GDACMDCNAM RQIDPNYLAW VLEELVEGRE RNVIEVDSEE
     AELAQVGLDR MLEL