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 04-NOV-2008, entry version 18. DE RecName: Full=Quinolinate synthetase A; GN Name=nadA; OrderedLocusNames=CD2372; OS Clostridium difficile (strain 630). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=272563; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a RT highly mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with CC dihydroxyacetone phosphate to form quinolinate (By similarity). CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; pyridine-2,3- CC dicarboxylate from iminoaspartate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the quinolinate synthetase A family. Type 2 CC subfamily. 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; YP_001088884.1; -. DR GeneID; 4914025; -. DR GenomeReviews; AM180355_GR; CD2372. DR KEGG; cdf:CD2372; -. DR NMPDR; fig|1496.1.peg.2476; -. DR HOGENOM; Q185P4; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0008987; F:quinolinate synthetase A activity; IEA:HAMAP. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00568; -; 1. DR InterPro; IPR003473; NadA. DR Pfam; PF02445; NadA; 1. DR TIGRFAMs; TIGR00550; nadA; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Pyridine nucleotide biosynthesis. FT CHAIN 1 304 Quinolinate synthetase A. FT /FTId=PRO_1000061150. 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 //