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 22-FEB-2012, entry version 44. DE RecName: Full=Quinolinate synthase A; DE EC=2.5.1.72; GN Name=nadA; OrderedLocusNames=CD630_23720; 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]. 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., 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 -!- CATALYTIC ACTIVITY: Glycerone phosphate + iminosuccinate = CC pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from iminoaspartate: step 1/1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the quinolinate synthase 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; NC_009089.1. DR ProteinModelPortal; Q185P4; -. DR STRING; Q185P4; -. DR GeneID; 4914025; -. DR GenomeReviews; AM180355_GR; CD2372. DR KEGG; cdf:CD2372; -. DR PATRIC; 19443205; VBICloDif38397_2489. DR eggNOG; COG0379; -. DR HOGENOM; HBG291157; -. DR KO; K03517; -. DR OMA; IAHPECE; -. DR ProtClustDB; PRK09375; -. 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:InterPro. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro. DR HAMAP; MF_00568; NadA_type2; 1; -. DR InterPro; IPR003473; NadA. DR InterPro; IPR023066; Quinolinate_synth_type2. 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; Transferase. FT CHAIN 1 304 Quinolinate synthase A. FT /FTId=PRO_1000061150. FT BINDING 23 23 Iminoaspartate (By similarity). FT BINDING 40 40 Iminoaspartate; via amide nitrogen (By FT similarity). FT BINDING 111 111 Iminoaspartate (By similarity). FT BINDING 128 128 Iminoaspartate (By similarity). FT BINDING 197 197 Iminoaspartate (By similarity). FT BINDING 214 214 Iminoaspartate (By similarity). 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 //