ID   NADA_STACT              Reviewed;         366 AA.
AC   B9DMZ6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Quinolinate synthase {ECO:0000255|HAMAP-Rule:MF_00569};
DE            EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00569};
GN   Name=nadA {ECO:0000255|HAMAP-Rule:MF_00569}; OrderedLocusNames=Sca_1404;
OS   Staphylococcus carnosus (strain TM300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=396513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM300;
RX   PubMed=19060169; DOI=10.1128/aem.01982-08;
RA   Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA   Goetz F.;
RT   "Genome analysis of the meat starter culture bacterium Staphylococcus
RT   carnosus TM300.";
RL   Appl. Environ. Microbiol. 75:811-822(2009).
CC   -!- FUNCTION: Catalyzes the condensation of iminoaspartate with
CC       dihydroxyacetone phosphate to form quinolinate. {ECO:0000255|HAMAP-
CC       Rule:MF_00569}.
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_00569};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25889;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00569};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00569};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00569};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from
CC       iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00569}.
CC   -!- SIMILARITY: Belongs to the quinolinate synthase family. Type 3
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00569}.
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DR   EMBL; AM295250; CAL28309.1; -; Genomic_DNA.
DR   RefSeq; WP_015900649.1; NC_012121.1.
DR   AlphaFoldDB; B9DMZ6; -.
DR   SMR; B9DMZ6; -.
DR   STRING; 396513.SCA_1404; -.
DR   GeneID; 60544910; -.
DR   KEGG; sca:SCA_1404; -.
DR   eggNOG; COG0379; Bacteria.
DR   HOGENOM; CLU_047382_2_0_9; -.
DR   OMA; FFLPDKC; -.
DR   OrthoDB; 613347at2; -.
DR   BioCyc; SCAR396513:SCA_RS07015-MON; -.
DR   UniPathway; UPA00253; UER00327.
DR   Proteomes; UP000000444; 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_00569; NadA_type3; 1.
DR   InterPro; IPR003473; NadA.
DR   InterPro; IPR036094; NadA_sf.
DR   InterPro; IPR023515; Quinolinate_synth_A_type3.
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..366
FT                   /note="Quinolinate synthase"
FT                   /id="PRO_1000146825"
FT   BINDING         44
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         61
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         108
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         139..141
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         160
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         228
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         254..256
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         271
FT                   /ligand="iminosuccinate"
FT                   /ligand_id="ChEBI:CHEBI:77875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
FT   BINDING         318
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00569"
SQ   SEQUENCE   366 AA;  41346 MW;  C8679E129DE8BA93 CRC64;
     MFNPILSVSK SIPEKYLQMS QEELENHIQA IKDQLGNRLF MPTHHYQKNE VVQFADITGD
     SLELARICKE NTEAEYFVFN GVHFMAETAD ILTDDSQDIY LPDLSAGCSM ADMANITQAL
     HGYDVLTEKF HLDILPLTYV NSTAAIKKFV GEHGGSCVTS GNAKSVVDWA LNQGKVILFL
     PDQHLGRNTA YDLGIPLEQM AVWDPIAKEL IYEGDLEDLR IVLWKGHCSV HEKFHKAHID
     MARERDPEIN VIVHPECEFE VVQAADYAGS TRYIIETIKN APKGSRWLIG TEMNLVNRLK
     ETYTDITIDS LNPLMCSCLT MNRIDLPHLA WCLDKILDGN KDNIIKVDAE TAKYAKESLD
     RMLSIT