ID NADA_HELPY Reviewed; 336 AA. AC O25910; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 124. 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}; GN OrderedLocusNames=HP_1356; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000511; AAD08398.1; -; Genomic_DNA. DR PIR; D64689; D64689. DR RefSeq; NP_208148.1; NC_000915.1. DR RefSeq; WP_001141770.1; NC_018939.1. DR AlphaFoldDB; O25910; -. DR SMR; O25910; -. DR DIP; DIP-3397N; -. DR IntAct; O25910; 1. DR MINT; O25910; -. DR STRING; 85962.HP_1356; -. DR PaxDb; 85962-C694_07000; -. DR DNASU; 900347; -. DR EnsemblBacteria; AAD08398; AAD08398; HP_1356. DR KEGG; hpy:HP_1356; -. DR PATRIC; fig|85962.47.peg.1452; -. DR eggNOG; COG0379; Bacteria. DR InParanoid; O25910; -. DR OrthoDB; 9801204at2; -. DR PhylomeDB; O25910; -. DR UniPathway; UPA00253; UER00327. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008987; F:quinolinate synthetase A activity; IBA:GO_Central. DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central. DR Gene3D; 3.40.50.10800; NadA-like; 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 NCBIfam; TIGR00550; nadA; 1. DR PANTHER; PTHR30573:SF0; QUINOLINATE SYNTHASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR30573; QUINOLINATE SYNTHETASE A; 1. DR Pfam; PF02445; NadA; 1. DR SUPFAM; SSF142754; NadA-like; 1. PE 3: Inferred from homology; KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1..336 FT /note="Quinolinate synthase" FT /id="PRO_0000155818" FT BINDING 25 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" FT BINDING 42 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" FT BINDING 86 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" FT BINDING 117..119 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" FT BINDING 138 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" FT BINDING 198 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" FT BINDING 224..226 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" FT BINDING 241 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" FT BINDING 288 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00569" SQ SEQUENCE 336 AA; 37813 MW; 963569A848239C4F CRC64; MPTDNDLKAA ILELLRDLDV LLVAHFYQKD EIVELAHYTG DSLELAKIAS QSDKNLIVFC GVHFMGESVK ALAFDKQVIM PKLSCCSMAR MIDSHYYDRS VHLLKECGVK EFYPITYINS NAEVKAKVAK DDGVVCTSRN ASKIFNHALK QNKKIFFLPD KCLGENLALE NGLKSAILGA NSQEEIKNAD VVCYNGFCSV HQLFKLEDIE FYRQKYPDIL IAVHPECEPS VVSNADFSGS TSQIIEFVEK LSPNQKVAIG TESHLVNRLK AKRHHQNTFI LSSTLALCPT MNETTLKDLF EVLKAYKNHR AYNTIELKDE VARLAKLALT KMMELS //