ID NADA_CLOD6 Reviewed; 304 AA. AC Q185P4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 25-MAY-2022, entry version 94. DE RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00568}; DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00568}; GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00568}; OrderedLocusNames=CD630_23720; OS Clostridioides difficile (strain 630) (Peptoclostridium difficile). OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae; OC Clostridioides. OX NCBI_TaxID=272563; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L., RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a highly RT mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP- CC Rule:MF_00568}. 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_00568}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00568}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00568}. 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; AM180355; CAJ69257.1; -; Genomic_DNA. DR RefSeq; WP_004454668.1; NZ_CP010905.2. DR RefSeq; YP_001088884.1; NC_009089.1. DR AlphaFoldDB; Q185P4; -. DR SMR; Q185P4; -. DR STRING; 272563.CD630_23720; -. DR PRIDE; Q185P4; -. DR EnsemblBacteria; CAJ69257; CAJ69257; CD630_23720. DR GeneID; 66354766; -. DR KEGG; cdf:CD630_23720; -. DR KEGG; pdc:CDIF630_02612; -. DR PATRIC; fig|272563.120.peg.2505; -. DR eggNOG; COG0379; Bacteria. DR OMA; CFCSTMN; -. DR PhylomeDB; Q185P4; -. DR UniPathway; UPA00253; UER00327. DR Proteomes; UP000001978; 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_00568; NadA_type2; 1. DR InterPro; IPR003473; NadA. DR InterPro; IPR036094; NadA_sf. DR InterPro; IPR023066; Quinolinate_synth_type2. 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; Reference proteome; Transferase. FT CHAIN 1..304 FT /note="Quinolinate synthase" FT /id="PRO_1000061150" FT REGION 111..113 FT /note="Iminoaspartate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" FT REGION 197..199 FT /note="Iminoaspartate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" FT METAL 85 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" FT METAL 171 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" FT METAL 259 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" FT BINDING 23 FT /note="Iminoaspartate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" FT BINDING 40 FT /note="Iminoaspartate; via amide nitrogen" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" FT BINDING 128 FT /note="Iminoaspartate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" FT BINDING 214 FT /note="Iminoaspartate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00568" SQ SEQUENCE 304 AA; 34397 MW; 6EEBCD5EE1FE7837 CRC64; MDKDLTYQIK ELKKEKNAII LAHFYQPPEI QELADAVGDS YYLSEIARDC KEEVVVFCGV RFMGESAKIL SPEKTVLMPV SNAGCAMADM VDEEGVIKLK QQYPNALVVC YINSTAKVKA HCDVSVTSSS AIKILENIDN KEIIFLPDKN LGGYIAEQFP DKNFIFWDGY CKYHNNIRAE EIIELKDKYK NAEVLVHPEC KKEIRDLGDY VGSTSGIIKY ATNSKNKDFI IATEEGILHE LKKNNPNKNF YIPGGKILCT DMKKTTLENL YSTLKNMENE VIVEDEIMEK ALNSLLNMHK LAEG //