ID   NADA_PROM3              Reviewed;         333 AA.
AC   A2C9Z7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=P9303_15631;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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}.
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DR   EMBL; CP000554; ABM78307.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C9Z7; -.
DR   SMR; A2C9Z7; -.
DR   STRING; 59922.P9303_15631; -.
DR   EnsemblBacteria; ABM78307; ABM78307; P9303_15631.
DR   KEGG; pmf:P9303_15631; -.
DR   HOGENOM; CLU_047382_0_0_3; -.
DR   OMA; FFLPDKC; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000002274; 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; Transferase.
FT   CHAIN           1..333
FT                   /note="Quinolinate synthase"
FT                   /id="PRO_1000129441"
FT   BINDING         41
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT   BINDING         58
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT   BINDING         103
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT   BINDING         129..131
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT   BINDING         146
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT   BINDING         189
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT   BINDING         215..217
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT   BINDING         232
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
FT   BINDING         282
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00568"
SQ   SEQUENCE   333 AA;  37299 MW;  84B8CA9E18521EDB CRC64;
     MVRMTAVCTA KTVSPVPSTR KEFKGAIAEL RKKLNAVILA HYYQDPEIQD IADFIGDSLE
     LSRRAASTNA DVIVFCGVHF MAETAKILSP EKIVLLPDLE AGCSLADDCP ADEFAAFRDK
     HPDHIVVSYI NCTAAVKAQS DLICTSSNAV ALVSQLPKDR PILFAPDQNL GRWVQKQSGR
     ELTIWPGRCM VHETFSEEAL LKLKMMHPEA KVIAHPECLE RLLELADYVG STSKLLEYTE
     TNPGTKFIVL TEPGILHQMK QRMPNKEFMD VPGIDGCSCN ECPYMRLNTL EKLWRCLSTM
     KPSIEIEEGV RQKALIPIQR MLNMKEKQEA SQH