ID NADA_RALPJ Reviewed; 382 AA. AC B2UAP5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00567}; DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00567}; GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00567}; GN OrderedLocusNames=Rpic_2717; OS Ralstonia pickettii (strain 12J). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=402626; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=12J; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.; RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with CC dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP- CC Rule:MF_00567}. 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_00567}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00567}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00567}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00567}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from CC iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00567}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00567}. CC -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00567}. 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; CP001068; ACD27842.1; -; Genomic_DNA. DR AlphaFoldDB; B2UAP5; -. DR SMR; B2UAP5; -. DR STRING; 402626.Rpic_2717; -. DR KEGG; rpi:Rpic_2717; -. DR PATRIC; fig|402626.5.peg.3853; -. DR eggNOG; COG0379; Bacteria. DR HOGENOM; CLU_047382_1_0_4; -. DR UniPathway; UPA00253; UER00327. 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; NadA-like; 3. DR HAMAP; MF_00567; NadA_type1; 1. DR InterPro; IPR003473; NadA. DR InterPro; IPR036094; NadA_sf. DR InterPro; IPR023513; Quinolinate_synth_A_type1. 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; Transferase. FT CHAIN 1..382 FT /note="Quinolinate synthase" FT /id="PRO_1000129421" FT BINDING 63 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" FT BINDING 84 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" FT BINDING 129 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" FT BINDING 155..157 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" FT BINDING 172 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" FT BINDING 216 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" FT BINDING 242..244 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" FT BINDING 259 FT /ligand="iminosuccinate" FT /ligand_id="ChEBI:CHEBI:77875" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" FT BINDING 313 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00567" SQ SEQUENCE 382 AA; 41479 MW; F30923B3576E56A5 CRC64; METHIKTVEF ERPDMLSEAQ SGASCVAHAW AKVPPVLSRE ERDELKARIK RLLKEREAVL VAHYYVDADL QDLAEETGGC VSDSLEMARF GRDHSAKTLI VAGVRFMGET AKILSPEKTV LMPDLDATCS LDLGCPPDEF AAFCDAHPDR TVVVYANTSA AVKARADWMV TSSIGLKIVQ HLHAQGKKIL WAPDRHLGSY IQKQTGADML MWQGSCLVHD EFKGVELDLL RAEHPNAKIL VHPESPESVV AQADVVGSTS QLIAAAQSLS AQEFIVATDN GILHKMRMAA PGKRFIEAPT AGNAATCKSC AHCPWMAMNA LTNLAEVLET GRNEIHVDPA IGRQAVVCID RMLDFAAREK ATVRPQGDLA ANAQLFQGIG PA //